malK

Summary

Gene Symbol: malK
Description: maltose ABC transportor ATPase
Alias: ECK4027, JW3995
Species: Escherichia coli str. K-12 substr. MG1655

Top Publications

  1. Lacour S, Bechet E, Cozzone A, Mijakovic I, Grangeasse C. Tyrosine phosphorylation of the UDP-glucose dehydrogenase of Escherichia coli is at the crossroads of colanic acid synthesis and polymyxin resistance. PLoS ONE. 2008;3:e3053 pubmed publisher
    ..coli to the antibiotic polymyxin. Ugd phosphorylation seems to be at the junction between two distinct biosynthetic pathways, illustrating the regulatory potential of tyrosine phosphorylation in bacterial physiology. ..
  2. Carlson M, Bao H, Duong F. Formation of a Chloride-conducting State in the Maltose ATP-binding Cassette (ABC) Transporter. J Biol Chem. 2016;291:12119-25 pubmed publisher
  3. Reich Slotky R, Panagiotidis C, Reyes M, Shuman H. The detergent-soluble maltose transporter is activated by maltose binding protein and verapamil. J Bacteriol. 2000;182:993-1000 pubmed
    ..This uncoupled activity was not due to dissociation of the MalK ATPase subunit from the integral membrane protein MalF and MalG subunits...
  4. Ferenci T. Methyl-alpha-maltoside and 5-thiomaltose: analogs transported by the Escherichia coli maltose transport system. J Bacteriol. 1980;144:7-11 pubmed
    ..Both analogs were inhibitory to the growth of E. coli, but only when the bacteria were previously induced for the maltose transport system. The analogs are substrates for but poor inducers of the maltose transport system. ..
  5. Newbury S, Smith N, Higgins C. Differential mRNA stability controls relative gene expression within a polycistronic operon. Cell. 1987;51:1131-43 pubmed
    ..The widespread occurrence of REP sequences and other sequences that could potentially stabilize upstream mRNA suggests that this mechanism of control of gene expression may be rather common...
  6. Newbury S, Smith N, Robinson E, Hiles I, Higgins C. Stabilization of translationally active mRNA by prokaryotic REP sequences. Cell. 1987;48:297-310 pubmed
    ..The implications of these findings for the mechanisms of mRNA degradation and for the role of RNA stability in the regulation of gene expression are discussed. ..
  7. Bukau B, Ehrmann M, Boos W. Osmoregulation of the maltose regulon in Escherichia coli. J Bacteriol. 1986;166:884-91 pubmed
    ..Mutants lacking MalK, a cytoplasmic membrane protein required for maltose transport, expressed the remaining mal genes at a high level, ..
  8. Dean D, Reizer J, Nikaido H, Saier M. Regulation of the maltose transport system of Escherichia coli by the glucose-specific enzyme III of the phosphoenolpyruvate-sugar phosphotransferase system. Characterization of inducer exclusion-resistant mutants and reconstitution of inducer exclus. J Biol Chem. 1990;265:21005-10 pubmed
    ..We have isolated and characterized four mutants in the maltose transport system, all of which are in malK, which are resistant to inducer exclusion...
  9. Landmesser H, Stein A, Blüschke B, Brinkmann M, Hunke S, Schneider E. Large-scale purification, dissociation and functional reassembly of the maltose ATP-binding cassette transporter (MalFGK(2)) of Salmonella typhimurium. Biochim Biophys Acta. 2002;1565:64-72 pubmed
    ..yield in purified complex protein by taking advantage of a newly constructed expression plasmid that carries the malK, malF and malG genes in tandem orientation...

More Information

Publications95

  1. Hunke S, Mourez M, Jehanno M, Dassa E, Schneider E. ATP modulates subunit-subunit interactions in an ATP-binding cassette transporter (MalFGK2) determined by site-directed chemical cross-linking. J Biol Chem. 2000;275:15526-34 pubmed
    ..superfamily, is composed of two integral membrane proteins, MalF and MalG, and of two copies of an ATPase subunit, MalK, which hydrolyze ATP, thus energizing the translocation process...
  2. Li C, Yang Y, Su J, Liu B, Tan J, Zhang X, et al. Allosteric transitions of the maltose transporter studied by an elastic network model. Biopolymers. 2014;101:758-68 pubmed publisher
    ..These results can provide some insights into the understanding of the mechanism of ABC transporters...
  3. Sharoar M, Shahnawaz M, Islam M, Ramasamy V, Shin S, Park I. The inhibitory effects of Escherichia coli maltose binding protein on ?-amyloid aggregation and cytotoxicity. Arch Biochem Biophys. 2013;538:41-8 pubmed publisher
    ..We speculate that inhibition of the growth rate of potent A?42 species by MBP suppresses A?42-mediated toxicity in SH-SY5Y cells. ..
  4. Sharff A, Rodseth L, Szmelcman S, Hofnung M, Quiocho F. Refined structures of two insertion/deletion mutants probe function of the maltodextrin binding protein. J Mol Biol. 1995;246:8-13 pubmed
    ..This is most likely due to the long distance of the mutation from the binding site and conservation of the number of interactions between the area around the deletion site and the main body of the protein. ..
  5. Ehrmann M, Beckwith J. Proper insertion of a complex membrane protein in the absence of its amino-terminal export signal. J Biol Chem. 1991;266:16530-3 pubmed
  6. Reidl J, Boos W. The malX malY operon of Escherichia coli encodes a novel enzyme II of the phosphotransferase system recognizing glucose and maltose and an enzyme abolishing the endogenous induction of the maltose system. J Bacteriol. 1991;173:4862-76 pubmed
    Mutants lacking MalK, a subunit of the binding protein-dependent maltose-maltodextrin transport system, constitutively express the maltose genes. A second site mutation in malI abolishes the constitutive expression...
  7. Mannering D, Sharma S, Davidson A. Demonstration of conformational changes associated with activation of the maltose transport complex. J Biol Chem. 2001;276:12362-8 pubmed
    ..transporter contains two transmembrane subunits, MalF and MalG, and two copies of a nucleotide-hydrolyzing subunit, MalK. Mutant transport complexes that function in the absence of binding protein are thought to be stabilized in an ..
  8. Rubin S, Lee S, Ruiz E, Pines A, Wemmer D. Detection and characterization of xenon-binding sites in proteins by 129Xe NMR spectroscopy. J Mol Biol. 2002;322:425-40 pubmed
    ..Further applications of 129Xe NMR to biochemical assays, including the screening of proteins for xenon binding for crystallography are considered...
  9. Oldham M, Khare D, Quiocho F, Davidson A, Chen J. Crystal structure of a catalytic intermediate of the maltose transporter. Nature. 2007;450:515-21 pubmed
    ..These results provide direct evidence for a concerted mechanism of transport in which solute is transferred from the binding protein to the transmembrane subunits when the cassette dimer closes to hydrolyse ATP...
  10. Treptow N, Shuman H. Genetic evidence for substrate and periplasmic-binding-protein recognition by the MalF and MalG proteins, cytoplasmic membrane components of the Escherichia coli maltose transport system. J Bacteriol. 1985;163:654-60 pubmed
    ..These results suggest that the malF and malG mutations result in exposure of a substrate recognition site that is usually available only to substrates bound to MBP...
  11. Nikaido H. Maltose transport system of Escherichia coli: an ABC-type transporter. FEBS Lett. 1994;346:55-8 pubmed
    ..MBP), the presumed transmembrane channel made up of MalF and MalG proteins, and two copies of the ATPase subunit, MalK. The membrane-associated transporter complex was purified in a functional form both from the wild-type strain and ..
  12. Steinke A, Grau S, Davidson A, Hofmann E, Ehrmann M. Characterization of transmembrane segments 3, 4, and 5 of MalF by mutational analysis. J Bacteriol. 2001;183:375-81 pubmed
    ..The phenotypes and locations of the mutations are consistent with a previously postulated structural model of MalF...
  13. Meyer D, Schneider Fresenius C, Horlacher R, Peist R, Boos W. Molecular characterization of glucokinase from Escherichia coli K-12. J Bacteriol. 1997;179:1298-306 pubmed
    ..that exhibited constitutive mal gene expression due to endogenous induction and, in the absence of a functional MalK protein, the ATP-hydrolyzing subunit of the maltose transport system...
  14. Ehrmann M, Boos W. Identification of endogenous inducers of the mal regulon in Escherichia coli. J Bacteriol. 1987;169:3539-45 pubmed
    ..Mutations in malK, which codes for a component of the transport system, result in the elevated expression of the remaining mal genes...
  15. Merino G, Shuman H. Unliganded maltose-binding protein triggers lactose transport in an Escherichia coli mutant with an alteration in the maltose transport system. J Bacteriol. 1997;179:7687-94 pubmed
    ..in the periplasm, and the proteins of the inner membrane complex (MalFGK2), composed of one MalF, one MalG, and two MalK subunits. Substrate specificity is determined primarily by the periplasmic component, MBP...
  16. Dassa E, Lambert P. Activity of protein MalE (maltose-binding protein) fused to cytoplasmic and periplasmic regions of an Escherichia coli inner membrane protein. Res Microbiol. 1997;148:389-95 pubmed
    ..We discuss the possibility of genetically determining the topology of cytoplasmic membrane proteins by a method based on engineered fusions to MBP...
  17. Daus M, Grote M, Schneider E. The MalF P2 loop of the ATP-binding cassette transporter MalFGK2 from Escherichia coli and Salmonella enterica serovar typhimurium interacts with maltose binding protein (MalE) throughout the catalytic cycle. J Bacteriol. 2009;191:754-61 pubmed publisher
    ..In particular, this loop is involved in keeping MalE in close contact with the transporter. The data are discussed with respect to a crystal structure and current transport models...
  18. Hor L, Shuman H. Genetic analysis of periplasmic binding protein dependent transport in Escherichia coli. Each lobe of maltose-binding protein interacts with a different subunit of the MalFGK2 membrane transport complex. J Mol Biol. 1993;233:659-70 pubmed
    ..membrane; the periplasmic maltose-binding protein (MBP); two integral inner membrane proteins, MalF and MalG; and MalK, which is associated with the cytoplasmic face of the inner membrane...
  19. Colonna B, Hofnung M. rho Mutations restore lamB expression in E. coli K12 strains with an inactive malB region. Mol Gen Genet. 1981;184:479-83 pubmed
    lamB, the structural gene for lambda receptor, is the second gene of the malK-lamB operon in the malB region of the Escherichia coli K12 chromosome...
  20. Merino G, Shuman H. Truncation of MalF results in lactose transport via the maltose transport system of Escherichia coli. J Biol Chem. 1998;273:2435-44 pubmed
    ..The mutant requires functional MalK-ATPase activity and hydrolyzes ATP constitutively. It also requires MalG...
  21. Mourez M, Jehanno M, Schneider E, Dassa E. In vitro interaction between components of the inner membrane complex of the maltose ABC transporter of Escherichia coli: modulation by ATP. Mol Microbiol. 1998;30:353-63 pubmed
    ..We focused on interactions between the nucleotide-binding protein, MalK, and the transmembrane proteins, MalF and MalG...
  22. Hall J, Davidson A, Nikaido H. Preparation and reconstitution of membrane-associated maltose transporter complex of Escherichia coli. Methods Enzymol. 1998;292:20-9 pubmed
  23. Silhavy T, Brickman E, Bassford P, Casadaban M, Shuman H, Schwartz V, et al. Structure of the malB region in Escherichia coli K12. II. Genetic map of the malE,F,G operon. Mol Gen Genet. 1979;174:249-59 pubmed
    Starting with a strain containing a malK-lacZ fusion, a series of lambda plaque-forming phages which carry varying amounts of the malE,F operon have been isolated. We have used these phages to construct a deletion map of the malE,F operon...
  24. Xu Y, Zheng Y, Fan J, Yang D. A new strategy for structure determination of large proteins in solution without deuteration. Nat Methods. 2006;3:931-7 pubmed
    ..The strategy extends the size limit for structure determination by NMR spectroscopy to 42 kDa for monomeric proteins and to 65 kDa for differentially labeled multimeric proteins without the need for deuteration or selective labeling. ..
  25. Hofnung M, Hatfield D, Schwartz M. malB region in Escherichia coli K-12: characterization of new mutations. J Bacteriol. 1974;117:40-7 pubmed
    ..for Mal(-)lambdas mutations (formerly called gene malB) in that region, into two adjacent genetic segments malJ and malK. malJ and malK are both involved in maltose permeation...
  26. Thirion J, Hofnung M. On some genetic aspects of phage lambda resistance in E. coli K12. Genetics. 1972;71:207-16 pubmed
    ..coli K12 genetic map. No trans dominant malT mutation have been found. Therefore if they exist, they occur at a frequency of less than 10(-8), or strongly reduce the growth rate of the mutants. ..
  27. Francoz E, Dassa E. 3' end of the malEFG operon in E.coli: localization of the transcription termination site. Nucleic Acids Res. 1988;16:4097-109 pubmed
    ..orf2 corresponds exactly to the 5' part of the xylE gene reported independently (Davis & Henderson, 1987) as the gene coding for the XylE protein, the xylose-proton symport of Escherichia coli. ..
  28. Hayashi T, Chiba S, Kaneta Y, Furuta T, Sakurai M. ATP-induced conformational changes of nucleotide-binding domains in an ABC transporter. Importance of the water-mediated entropic force. J Phys Chem B. 2014;118:12612-20 pubmed publisher
    ..This interpretation of the NBD dimerization mechanism in concert with ATP, especially focused on the water-mediated entropy force, is potentially applicable to a wide variety of the ABC transporters. ..
  29. Telmer P, Shilton B. Insights into the conformational equilibria of maltose-binding protein by analysis of high affinity mutants. J Biol Chem. 2003;278:34555-67 pubmed
  30. Schlegel A, BOHM A, Lee S, Peist R, Decker K, Boos W. Network regulation of the Escherichia coli maltose system. J Mol Microbiol Biotechnol. 2002;4:301-7 pubmed
    ..Transport controls the interaction of MalK and MalT thus affecting gene expression...
  31. Schlegel A, Danot O, Richet E, Ferenci T, Boos W. The N terminus of the Escherichia coli transcription activator MalT is the domain of interaction with MalY. J Bacteriol. 2002;184:3069-77 pubmed
    ..b>MalK, the ATP-hydrolyzing subunit of the cognate ABC transporter, MalY, an enzyme with the activity of a cystathionase, ..
  32. Davidson A, Shuman H, Nikaido H. Mechanism of maltose transport in Escherichia coli: transmembrane signaling by periplasmic binding proteins. Proc Natl Acad Sci U S A. 1992;89:2360-4 pubmed
    ..The products of the malF, malG, and malK genes form a membrane-associated complex that catalyzes the hydrolysis of ATP to provide energy for the transport ..
  33. Daus M, Berendt S, Wuttge S, Schneider E. Maltose binding protein (MalE) interacts with periplasmic loops P2 and P1 respectively of the MalFG subunits of the maltose ATP binding cassette transporter (MalFGK(2)) from Escherichia coli/Salmonella during the transport cycle. Mol Microbiol. 2007;66:1107-22 pubmed
    ..MalFGK(2)), comprising the pore-forming hydrophobic subunits, MalF and MalG, and two copies of the ABC subunit, MalK. We report on the isolation of suppressor mutations within malFG that partially restore transport of a maltose-..
  34. Bedouelle H, Hofnung M. A DNA sequence containing the control regions of the malEFG and malK-lamB operons in Escherichia coli K12. Mol Gen Genet. 1982;185:82-7 pubmed
    The malB region in E. coli is composed of two operons, malEFG and malK-lamB, transcribed divergently from a control region located between the malE and malK genes...
  35. Ohsumi M, Sekiya T, Nishimura S, Ohki M. Nucleotide sequence of the regulatory region of malB operons in E. coli. J Biochem. 1983;94:243-7 pubmed
    ..The region of malK, the proximal gene of the malKlamB operon, was deduced from the observation that a cloned segment contains an amino-..
  36. Srinivasan U, Iyer G, Przybycien T, Samsonoff W, Bell J. Crystine: fibrous biomolecular material from protein crystals cross-linked in a specific geometry. Protein Eng. 2002;15:895-902 pubmed
    ..Crystine fibers are a new type of biomolecular material with potential applications wherever the use of proteins in a fibrous form is desirable, for example, the incorporation of enzymes into cloth or filtration material. ..
  37. Clausen T, Schlegel A, Peist R, Schneider E, Steegborn C, Chang Y, et al. X-ray structure of MalY from Escherichia coli: a pyridoxal 5'-phosphate-dependent enzyme acting as a modulator in mal gene expression. EMBO J. 2000;19:831-42 pubmed
    ..Therefore, we propose that a direct protein-protein interaction with MalT, the central transcriptional activator of the maltose system, underlies MalY-dependent repression of the maltose system. ..
  38. Richet E. On the role of the multiple regulatory elements involved in the activation of the Escherichia coli malEp promoter. J Mol Biol. 1996;264:852-62 pubmed
    ..Some elements of this structure, namely the CRP site 1, located at -76.5, and the distal MalT sites, seem to play a direct role in malEp activation besides their participation in the assembly of the higher-order structure...
  39. Joly N, BOHM A, Boos W, Richet E. MalK, the ATP-binding cassette component of the Escherichia coli maltodextrin transporter, inhibits the transcriptional activator malt by antagonizing inducer binding. J Biol Chem. 2004;279:33123-30 pubmed
    b>MalK, the ATP-binding cassette component of the Escherichia coli maltodextrin transporter, has long been known to control negatively the activity of MalT, a transcriptional activator dedicated to the maltose regulon...
  40. Dassa E, Muir S. Membrane topology of MalG, an inner membrane protein from the maltose transport system of Escherichia coli. Mol Microbiol. 1993;7:29-38 pubmed
    ..transport system for maltose and maltodextrins is composed of five proteins--LamB, MalE, MalF, MalG and MalK--located in the three layers of the bacterial envelope...
  41. Oloo E, Fung E, Tieleman D. The dynamics of the MgATP-driven closure of MalK, the energy-transducing subunit of the maltose ABC transporter. J Biol Chem. 2006;281:28397-407 pubmed
    ..used molecular dynamics simulations to study the ATP-driven association of the NBDs of the maltose ABC transporter, MalK, based on the crystal structures of its open and semiopen dimers...
  42. Chapon C. Role of the catabolite activator protein in the maltose regulon of Escherichia coli. J Bacteriol. 1982;150:722-9 pubmed
    ..In the resulting strains, the expression of two of the maltose operons, malEFG and malK-lamB, still required the action of CAP, whereas that of the third operon, malPQ, was CAP independent...
  43. Schreiber V, Steegborn C, Clausen T, Boos W, Richet E. A new mechanism for the control of a prokaryotic transcriptional regulator: antagonistic binding of positive and negative effectors. Mol Microbiol. 2000;35:765-76 pubmed
    ..Together, these results establish that MalY acts directly upon MalT without the help of any factor, and that MalY is a negative effector of MalT competing with the inducer for MalT binding. ..
  44. Vidal Ingigliardi D, Raibaud O. Three adjacent binding sites for cAMP receptor protein are involved in the activation of the divergent malEp-malKp promoters. Proc Natl Acad Sci U S A. 1991;88:229-33 pubmed
    The divergent malEFG and malK-lamB-malM operons in Escherichia coli are controlled by partially overlapping promoters, whose activity depends on the presence of two transcriptional activators, MalT and the cAMP receptor protein (CRP)...
  45. Rousset J, Gilson E, Hofnung M. malM, a new gene of the maltose regulon in Escherichia coli K12. II. Mutations affecting the signal peptide of the MalM protein. J Mol Biol. 1986;191:313-20 pubmed
    malM is the last gene of the malK-lamB-malM operon of Escherichia coli K12. It encodes a periplasmic protein. Mutations affecting the hydrophobic core of the N-terminal extension of the MalM protein have been isolated...
  46. Boyd D, Manoil C, Beckwith J. Determinants of membrane protein topology. Proc Natl Acad Sci U S A. 1987;84:8525-9 pubmed
    ..These studies in conjunction with our earlier results show that alkaline phosphatase fusions to membrane proteins can be an important aid in analyzing membrane topology and its determinants...
  47. Daus M, Grote M, Muller P, Doebber M, Herrmann A, Steinhoff H, et al. ATP-driven MalK dimer closure and reopening and conformational changes of the "EAA" motifs are crucial for function of the maltose ATP-binding cassette transporter (MalFGK2). J Biol Chem. 2007;282:22387-96 pubmed
    ..a heterodimer of the hydrophobic subunits MalF and MalG constituting the translocation pore and of a homodimer of MalK, representing the ATP-hydrolyzing subunit...
  48. Dean D, Hor L, Shuman H, Nikaido H. Interaction between maltose-binding protein and the membrane-associated maltose transporter complex in Escherichia coli. Mol Microbiol. 1992;6:2033-40 pubmed
    ..coli requires the presence of both maltose-binding protein (MBP) in the periplasm and a complex of MalF, MalG, and MalK proteins (FGK2) located in the cytoplasmic membrane...
  49. Panagiotidis C, Shuman H. Maltose transport in Escherichia coli: mutations that uncouple ATP hydrolysis from transport. Methods Enzymol. 1998;292:30-9 pubmed
  50. Fetsch E, Davidson A. Maltose transport through the inner membrane of E. coli. Front Biosci. 2003;8:d652-60 pubmed
    ..This review discusses the current knowledge of the mechanism of maltose transport, as it relates to the ABC superfamily of transporters as a whole. ..
  51. Mourez M, Skouloubris S, Betton J, Dassa E. Heat shock induction by a misassembled cytoplasmic membrane protein complex in Escherichia coli. Mol Microbiol. 1997;26:821-31 pubmed
    ..Moreover, the observation of the phtrA induction by MalF could be a useful new tool for studying the insertion and assembly of the MalFGK2 complex...
  52. Stern M, Ames G, Smith N, Robinson E, Higgins C. Repetitive extragenic palindromic sequences: a major component of the bacterial genome. Cell. 1984;37:1015-26 pubmed
    ..Possible roles for the REP sequence in mRNA degradation, chromosome structure, and recombination are discussed. ..
  53. Kainosho M, Torizawa T, Iwashita Y, Terauchi T, Mei Ono A, Güntert P. Optimal isotope labelling for NMR protein structure determinations. Nature. 2006;440:52-7 pubmed
    ..It thus makes a large class of proteins newly accessible to detailed solution structure determination. ..
  54. Telmer P, Shilton B. Structural studies of an engineered zinc biosensor reveal an unanticipated mode of zinc binding. J Mol Biol. 2005;354:829-40 pubmed
    ..A comparison to the mechanism of maltose-induced domain rearrangement is discussed. ..
  55. Sharma S, Davis J, Ayvaz T, Traxler B, Davidson A. Functional reassembly of the Escherichia coli maltose transporter following purification of a MalF-MalG subassembly. J Bacteriol. 2005;187:2908-11 pubmed
    Taking advantage of a chaperone-like function of MalK, a stable complex of MalF-MalG could be solubilized from the Escherichia coli membrane and purified in high yield in the absence of MalK...
  56. Mueller G, Choy W, Yang D, Forman Kay J, Venters R, Kay L. Global folds of proteins with low densities of NOEs using residual dipolar couplings: application to the 370-residue maltodextrin-binding protein. J Mol Biol. 2000;300:197-212 pubmed
    ..When applied to experimental data recorded on MBP the precision of the family of structures generated improves from 5.5 to 2.2 A, while the rmsd with respect to the X-ray structure (1dmb) is reduced from 5.1 to 3.3 A. ..
  57. Dahl M, Francoz E, Saurin W, Boos W, Manson M, Hofnung M. Comparison of sequences from the malB regions of Salmonella typhimurium and Enterobacter aerogenes with Escherichia coli K12: a potential new regulatory site in the interoperonic region. Mol Gen Genet. 1989;218:199-207 pubmed
    The malE and malK genes from Salmonella typhimurium, and the malEFG operon and a portion of malK from Enterobacter aerogenes were cloned and sequenced. Plasmid-borne malE genes from both species and the malF and malG genes from E...
  58. Lv X, Liu H, Chen H, Gong H. Coupling between ATP hydrolysis and protein conformational change in maltose transporter. Proteins. 2017;85:207-220 pubmed publisher
    As the intracellular part of maltose transporter, MalK dimer utilizes the energy of ATP hydrolysis to drive protein conformational change, which then facilitates substrate transport...
  59. Jacso T, Grote M, Daus M, Schmieder P, Keller S, Schneider E, et al. Periplasmic loop P2 of the MalF subunit of the maltose ATP binding cassette transporter is sufficient to bind the maltose binding protein MalE. Biochemistry. 2009;48:2216-25 pubmed publisher
    ..In particular, a conformational change of domain 2 of MalF-P2 is induced, which is distinct from the conformation found in the X-ray structure...
  60. Oldham M, Chen J. Snapshots of the maltose transporter during ATP hydrolysis. Proc Natl Acad Sci U S A. 2011;108:15152-6 pubmed publisher
  61. Bao H, Duong F. Phosphatidylglycerol directs binding and inhibitory action of EIIAGlc protein on the maltose transporter. J Biol Chem. 2013;288:23666-74 pubmed publisher
    ..Using protein docking prediction and chemical cross-linking, we demonstrate that EIIA(Glc) binds to the MalK dimer, interacting with both the nucleotide-binding and the C-terminal regulatory domains...
  62. Raibaud O, Clement J, Hofnung M. Structure of the malB region in Escherichia coli K12. III. Correlation of the genetic map with the restriction map. Mol Gen Genet. 1979;174:261-7 pubmed
    ..This also allowed to localize the boundaries between malF and malE, malE and malK, mal K and lamB on the restriction map. The genetic map is not grossly distorted with respect to the physical map.
  63. Wandersman C, Schwartz M, Ferenci T. Escherichia coli mutants impaired in maltodextrin transport. J Bacteriol. 1979;140:1-13 pubmed
    ..They were defective in the transfer of maltodextrins from the periplasmic space to the cytoplasm but only slightly affected in the transport of maltose. ..
  64. Decker K, Plumbridge J, Boos W. Negative transcriptional regulation of a positive regulator: the expression of malT, encoding the transcriptional activator of the maltose regulon of Escherichia coli, is negatively controlled by Mlc. Mol Microbiol. 1998;27:381-90 pubmed
    ..MalT, the transcriptional activator of the system, is necessary for the transcription of all mal genes. MalK, the energy-transducing subunit of the transport system, acts phenotypically as repressor, particularly when ..
  65. Randall L, Hardy S, Josefsson L. Precursors of three exported proteins in Escherichia coli. Proc Natl Acad Sci U S A. 1978;75:1209-12 pubmed
    ..In contrast to the above, when the intracellular protein elongation factor Tu is synthesized in vitro on free polysomes, it is not detectably larger than the authentic form. ..
  66. Kühnau S, Reyes M, Sievertsen A, Shuman H, Boos W. The activities of the Escherichia coli MalK protein in maltose transport, regulation, and inducer exclusion can be separated by mutations. J Bacteriol. 1991;173:2180-6 pubmed
    ..Five proteins make up a periplasmic binding-protein-dependent active transport system. One of these proteins, MalK, contains an ATP-binding site and is thought to couple the hydrolysis of ATP to the accumulation of substrate...
  67. Davidson A, Nikaido H. Purification and characterization of the membrane-associated components of the maltose transport system from Escherichia coli. J Biol Chem. 1991;266:8946-51 pubmed
    ..The three membrane-associated components of the transport system, the MalK, MalF, and MalG proteins, have been solubilized from the membrane and maltose transport activity has been ..
  68. Martineau P, Saurin W, Hofnung M, Spurlino J, Quiocho F. Progress in the identification of interaction sites on the periplasmic maltose binding protein from E coli. Biochimie. 1990;72:397-402 pubmed
    ..Because of the structural similarities between periplasmic binding proteins, the regions of interaction defined could be relevant for other members of this family...
  69. Dean D, Davidson A, Nikaido H. The role of ATP as the energy source for maltose transport in Escherichia coli. Res Microbiol. 1990;141:348-52 pubmed
  70. Stein A, Seifert M, Volkmer Engert R, Siepelmeyer J, Jahreis K, Schneider E. Functional characterization of the maltose ATP-binding-cassette transporter of Salmonella typhimurium by means of monoclonal antibodies directed against the MalK subunit. Eur J Biochem. 2002;269:4074-85 pubmed
    ..These activities are thought to be mediated by interactions of the ATPase subunit, MalK, with the transcriptional activator, MalT, and nonphosphorylated enzyme IIA of the glucose phosphotransferase ..
  71. Grote M, Polyhach Y, Jeschke G, Steinhoff H, Schneider E, Bordignon E. Transmembrane signaling in the maltose ABC transporter MalFGK2-E: periplasmic MalF-P2 loop communicates substrate availability to the ATP-bound MalK dimer. J Biol Chem. 2009;284:17521-6 pubmed publisher
    ..92, 205, 239, 252, and 273 and one triple mutant labeled at positions 205/252 in P2 and 83 in the Q-loop of MalK were assayed...
  72. McGovern K, Ehrmann M, Beckwith J. Decoding signals for membrane protein assembly using alkaline phosphatase fusions. EMBO J. 1991;10:2773-82 pubmed
    ..The strength of cytoplasmic domains as topogenic signals varies, correlated with the density of positively charged amino acids within them...
  73. Shuman H, Panagiotidis C. Tinkering with transporters: periplasmic binding protein-dependent maltose transport in E. coli. J Bioenerg Biomembr. 1993;25:613-20 pubmed
  74. Bedouelle H, Schmeissner U, Hofnung M, Rosenberg M. Promoters of the malEFG and malK-lamB operons in Escherichia coli K12. J Mol Biol. 1982;161:519-31 pubmed
  75. Ferenci T. The recognition of maltodextrins by Escherichia coli. Eur J Biochem. 1980;108:631-6 pubmed
    ..The inability to transport dextrins larger than maltoheptaose is, therefore, due to the inability of E. coli to transfer large substrates from the binding protein to the cytoplasm and not to lack of access through the outer membrane. ..
  76. Shuman H, Silhavy T. Identification of the malK gene product. A peripheral membrane component of the Escherichia coli maltose transport system. J Biol Chem. 1981;256:560-2 pubmed
    The malK gene product of Escherichia coli has been identified through the use of a previously described technique that employs gene fusions (Shuman, H. A., Silhavy, T. J., and Beckwith, J. R. (1980) J. Biol. Chem. 255, 168-174)...
  77. Oldham M, Chen J. Crystal structure of the maltose transporter in a pretranslocation intermediate state. Science. 2011;332:1202-5 pubmed publisher
    ..that interactions with substrate-loaded maltose-binding protein in the periplasm induce a partial closure of the MalK dimer in the cytoplasm. ATP binding to this conformation then promotes progression to the outward-facing state...
  78. Schneider E, Hunke S, Tebbe S. The MalK protein of the ATP-binding cassette transporter for maltose of Escherichia coli is accessible to protease digestion from the periplasmic side of the membrane. J Bacteriol. 1995;177:5364-7 pubmed
    The ATP-hydrolyzing subunit MalK of the ATP-binding cassette transporter for maltose of Escherichia coli is demonstrated to be accessible to digestion by proteinase K in right-side-out membrane vesicles...
  79. Tchetina E, Newman E. Identification of Lrp-regulated genes by inverse PCR and sequencing: regulation of two mal operons of Escherichia coli by leucine-responsive regulatory protein. J Bacteriol. 1995;177:2679-83 pubmed
    ..This technique revealed that malT, malEFG, and malB-lamB-malK are all activated two- to fivefold by Lrp and confirmed that Lrp regulates expression of the leuDBCA and livHJKG ..
  80. Higgins C, Hiles I, Whalley K, Jamieson D. Nucleotide binding by membrane components of bacterial periplasmic binding protein-dependent transport systems. EMBO J. 1985;4:1033-9 pubmed
    ..site on one of the membrane components from each of three independent transport systems, the hisP, malK and oppD proteins of the histidine, maltose and oligopeptide permeases, respectively...
  81. Bechtluft P, van Leeuwen R, Tyreman M, Tomkiewicz D, Nouwen N, Tepper H, et al. Direct observation of chaperone-induced changes in a protein folding pathway. Science. 2007;318:1458-61 pubmed
    ..It appears that SecB only binds to the extended or molten globulelike structure and retains MBP in this latter state. Thus during MBP translocation, no energy is required to disrupt stable tertiary interactions. ..
  82. Duplay P, Szmelcman S, Bedouelle H, Hofnung M. Silent and functional changes in the periplasmic maltose-binding protein of Escherichia coli K12. I. Transport of maltose. J Mol Biol. 1987;194:663-73 pubmed
    ..A region near the C-terminal end is important for maltose binding. Two regions of the mature protein (residues 18 to 42 and 280 to 296) are required for export to, or solubility in, the periplasm...
  83. Treptow N, Shuman H. Allele-specific malE mutations that restore interactions between maltose-binding protein and the inner-membrane components of the maltose transport system. J Mol Biol. 1988;202:809-22 pubmed
    ..LamB, a periplasmic maltose-binding protein (MalE, MBP) and three inner-membrane proteins, MalF, MalG and MalK. MalF and MalG are integral transmembrane proteins, while MalK is associated with the inner aspect of the ..
  84. Ehrle R, Pick C, Ulrich R, Hofmann E, Ehrmann M. Characterization of transmembrane domains 6, 7, and 8 of MalF by mutational analysis. J Bacteriol. 1996;178:2255-62 pubmed
    ..The majority of mutations in membrane-spanning segment 8 caused a Mal+ Dex- phenotype. Six Mal+ suppressor mutations isolated to two mutations in transmembrane domain 7 changed amino acid residues in membrane-spanning segment 6 or 8...
  85. Davidson A, Sharma S. Mutation of a single MalK subunit severely impairs maltose transport activity in Escherichia coli. J Bacteriol. 1997;179:5458-64 pubmed
    ..binding protein and a membrane-associated translocation complex that contains two copies of the ATP-binding protein MalK. To examine the need for two nucleotide-binding domains in this transport complex, one of the two MalK subunits was ..
  86. Raibaud O, Roa M, Braun Breton C, Schwartz M. Structure of the malB region in Escherichia coli K12. I. Genetic map of the malK-lamB operon. Mol Gen Genet. 1979;174:241-8 pubmed
    A series of deletions, Mu insertions and point mutations affecting the malK-lamB operon have been isolated. They were used to establish a deletion map of this operon, which could be divided in 27 intervals, with 16 in malK and 11 in lamB...