adk

Summary

Gene Symbol: adk
Description: adenylate kinase
Alias: ECK0468, JW0463, dnaW, plsA
Species: Escherichia coli str. K-12 substr. MG1655
Products:     adk

Top Publications

  1. Muller C, Schulz G. Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9 A resolution. A model for a catalytic transition state. J Mol Biol. 1992;224:159-77 pubmed
    ..The mutants were classified. The concomitant increase of the Michaelis constants for ATP and AMP in the group of mutants that modify only the ATP-binding site cannot be explained. ..
  2. Muller C, Schlauderer G, Reinstein J, Schulz G. Adenylate kinase motions during catalysis: an energetic counterweight balancing substrate binding. Structure. 1996;4:147-56 pubmed
    ..This counterweight prevents the enzyme from dropping into a rate-reducing energy well along the reaction coordinate. ..
  3. Glembotski C, Chapman A, Atkinson D. Adenylate energy charge in Escherichia coli CR341T28 and properties of heat-sensitive adenylate kinase. J Bacteriol. 1981;145:1374-85 pubmed
  4. Maragakis P, Karplus M. Large amplitude conformational change in proteins explored with a plastic network model: adenylate kinase. J Mol Biol. 2005;352:807-22 pubmed
    ..0 A of the pathway, which corresponds to a conformational change between two end structures that differ by a C(alpha)-atom root-mean-squared deviation of 7.1A. ..
  5. Potestio R, Pontiggia F, Micheletti C. Coarse-grained description of protein internal dynamics: an optimal strategy for decomposing proteins in rigid subunits. Biophys J. 2009;96:4993-5002 pubmed publisher
    ..The known catalytic site of these enzymes is found to be preferentially located close to the boundary separating the two primary dynamical subdomains. ..
  6. Berry M, Bae E, Bilderback T, Glaser M, Phillips G. Crystal structure of ADP/AMP complex of Escherichia coli adenylate kinase. Proteins. 2006;62:555-6 pubmed
  7. Brune M, Schumann R, Wittinghofer F. Cloning and sequencing of the adenylate kinase gene (adk) of Escherichia coli. Nucleic Acids Res. 1985;13:7139-51 pubmed
    Adenylate kinase, the product of the adk locus in Escherichia coli K12, catalyzes the conversion of AMP and ATP to two molecules of ADP. The gene has been cloned by complementation of an adk temperature sensitive mutation...
  8. Sinev M, Sineva E, Ittah V, Haas E. Domain closure in adenylate kinase. Biochemistry. 1996;35:6425-37 pubmed
    ..The data confirmed the proposed stepwise manner of the domain closure of the enzyme and revealed the presence of multiple conformations of E. coli AK in solution. ..
  9. Berry M, Meador B, Bilderback T, Liang P, Glaser M, Phillips G. The closed conformation of a highly flexible protein: the structure of E. coli adenylate kinase with bound AMP and AMPPNP. Proteins. 1994;19:183-98 pubmed
    ..Finally, a comparison is made between the present structure and the structure of the heavy chain of muscle myosin. ..
  10. Muller C, Schulz G. Crystal structures of two mutants of adenylate kinase from Escherichia coli that modify the Gly-loop. Proteins. 1993;15:42-9 pubmed

Detail Information

Publications82

  1. Muller C, Schulz G. Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9 A resolution. A model for a catalytic transition state. J Mol Biol. 1992;224:159-77 pubmed
    ..The mutants were classified. The concomitant increase of the Michaelis constants for ATP and AMP in the group of mutants that modify only the ATP-binding site cannot be explained. ..
  2. Muller C, Schlauderer G, Reinstein J, Schulz G. Adenylate kinase motions during catalysis: an energetic counterweight balancing substrate binding. Structure. 1996;4:147-56 pubmed
    ..This counterweight prevents the enzyme from dropping into a rate-reducing energy well along the reaction coordinate. ..
  3. Glembotski C, Chapman A, Atkinson D. Adenylate energy charge in Escherichia coli CR341T28 and properties of heat-sensitive adenylate kinase. J Bacteriol. 1981;145:1374-85 pubmed
  4. Maragakis P, Karplus M. Large amplitude conformational change in proteins explored with a plastic network model: adenylate kinase. J Mol Biol. 2005;352:807-22 pubmed
    ..0 A of the pathway, which corresponds to a conformational change between two end structures that differ by a C(alpha)-atom root-mean-squared deviation of 7.1A. ..
  5. Potestio R, Pontiggia F, Micheletti C. Coarse-grained description of protein internal dynamics: an optimal strategy for decomposing proteins in rigid subunits. Biophys J. 2009;96:4993-5002 pubmed publisher
    ..The known catalytic site of these enzymes is found to be preferentially located close to the boundary separating the two primary dynamical subdomains. ..
  6. Berry M, Bae E, Bilderback T, Glaser M, Phillips G. Crystal structure of ADP/AMP complex of Escherichia coli adenylate kinase. Proteins. 2006;62:555-6 pubmed
  7. Brune M, Schumann R, Wittinghofer F. Cloning and sequencing of the adenylate kinase gene (adk) of Escherichia coli. Nucleic Acids Res. 1985;13:7139-51 pubmed
    Adenylate kinase, the product of the adk locus in Escherichia coli K12, catalyzes the conversion of AMP and ATP to two molecules of ADP. The gene has been cloned by complementation of an adk temperature sensitive mutation...
  8. Sinev M, Sineva E, Ittah V, Haas E. Domain closure in adenylate kinase. Biochemistry. 1996;35:6425-37 pubmed
    ..The data confirmed the proposed stepwise manner of the domain closure of the enzyme and revealed the presence of multiple conformations of E. coli AK in solution. ..
  9. Berry M, Meador B, Bilderback T, Liang P, Glaser M, Phillips G. The closed conformation of a highly flexible protein: the structure of E. coli adenylate kinase with bound AMP and AMPPNP. Proteins. 1994;19:183-98 pubmed
    ..Finally, a comparison is made between the present structure and the structure of the heavy chain of muscle myosin. ..
  10. Muller C, Schulz G. Crystal structures of two mutants of adenylate kinase from Escherichia coli that modify the Gly-loop. Proteins. 1993;15:42-9 pubmed
  11. Kubitzki M, de Groot B. The atomistic mechanism of conformational transition in adenylate kinase: a TEE-REX molecular dynamics study. Structure. 2008;16:1175-82 pubmed publisher
    ..molecular dynamics simulation of the complete conformational transition of Escherichia coli adenylate kinase (ADK) using the recently developed TEE-REX algorithm...
  12. Henzler Wildman K, Lei M, Thai V, Kerns S, Karplus M, Kern D. A hierarchy of timescales in protein dynamics is linked to enzyme catalysis. Nature. 2007;450:913-6 pubmed
    ..The connection between different timescales and the corresponding amplitudes of motions in adenylate kinase and their linkage to catalytic function is likely to be a general characteristic of protein energy landscapes. ..
  13. Snow C, Qi G, Hayward S. Essential dynamics sampling study of adenylate kinase: comparison to citrate synthase and implication for the hinge and shear mechanisms of domain motions. Proteins. 2007;67:325-37 pubmed
    ..In general though it appears a bias toward keeping the unliganded enzyme in the open-domain conformation may be a common feature of domain enzymes. ..
  14. Whitford P, Miyashita O, Levy Y, Onuchic J. Conformational transitions of adenylate kinase: switching by cracking. J Mol Biol. 2007;366:1661-71 pubmed
    ..We further characterize the conformational transitions with a new measure Phi(Func), and demonstrate that local unfolding may be due, in part, to competing intra-protein interactions. ..
  15. Krishnamurthy H, Lou H, Kimple A, Vieille C, Cukier R. Associative mechanism for phosphoryl transfer: a molecular dynamics simulation of Escherichia coli adenylate kinase complexed with its substrates. Proteins. 2005;58:88-100 pubmed
  16. Shapiro Y, Sinev M, Sineva E, Tugarinov V, Meirovitch E. Backbone dynamics of escherichia coli adenylate kinase at the extreme stages of the catalytic cycle studied by (15)N NMR relaxation. Biochemistry. 2000;39:6634-44 pubmed
    ..The hypothesis of energetic counter balancing of substrate binding based on crystallographic data is strongly supported by the solution NMR results. Correlations between backbone dynamics and domain displacement are established. ..
  17. Temiz N, Meirovitch E, Bahar I. Escherichia coli adenylate kinase dynamics: comparison of elastic network model modes with mode-coupling (15)N-NMR relaxation data. Proteins. 2004;57:468-80 pubmed
    ..It is shown that NMR/SRLS and GNM/ANM analyses can be advantageously synthesized to provide insights into the molecular mechanisms that control biological function. ..
  18. Cronan J, Ray T, Vagelos P. Selection and characterization of an E. coli mutant defective in membrane lipid biosynthesis. Proc Natl Acad Sci U S A. 1970;65:737-44 pubmed
    ..The phenotype of this mutant appears due to a single mutation by reversion analysis and by enzymatic analysis of temperature-resistant revertants. ..
  19. Daily M, Phillips G, Cui Q. Many local motions cooperate to produce the adenylate kinase conformational transition. J Mol Biol. 2010;400:618-31 pubmed publisher
    ..Finally, the analytical approach and the insights derived from this work may inform the rational design of flexibility and allostery in proteins. ..
  20. Ratner V, Kahana E, Haas E. The natively helical chain segment 169-188 of Escherichia coli adenylate kinase is formed in the latest phase of the refolding transition. J Mol Biol. 2002;320:1135-45 pubmed
    ..The helical conformation of this segment is established only in the second, much slower, refolding phase, simultaneously with the completion of the native structure. ..
  21. Lin Y, Nageswara Rao B. Structural characterization of adenine nucleotides bound to Escherichia coli adenylate kinase. 1. Adenosine conformations by proton two-dimensional transferred nuclear Overhauser effect spectroscopy. Biochemistry. 2000;39:3636-46 pubmed
    ..N. , Jr. (1994) Proteins: Struct., Funct., Genet. 19, 183-198], showed that polarization transfer to the protein protons does not produce significant errors in the structures determined by considering the ligand NOEs alone. ..
  22. Sinev M, Sineva E, Ittah V, Haas E. Towards a mechanism of AMP-substrate inhibition in adenylate kinase from Escherichia coli. FEBS Lett. 1996;397:273-6 pubmed
    ..Closure of the LID domain in response to AMP binding may be a possible reason for the strong AMP-substrate inhibition known for E. coli AK. ..
  23. Ishige K, Noguchi T. Inorganic polyphosphate kinase and adenylate kinase participate in the polyphosphate:AMP phosphotransferase activity of Escherichia coli. Proc Natl Acad Sci U S A. 2000;97:14168-71 pubmed
    ..PPK and adenylate kinase form a complex in the presence of polyphosphate. We discuss a phosphotransfer mechanism that involves both enzymes and enables polyP to be a phospho-donor to AMP. ..
  24. Ratner V, Kahana E, Eichler M, Haas E. A general strategy for site-specific double labeling of globular proteins for kinetic FRET studies. Bioconjug Chem. 2002;13:1163-70 pubmed
    ..The procedure described herein is a general outline of procedures, which can meet the double challenge of both site specificity and large-scale preparation of doubly labeled proteins. ..
  25. Lou H, Cukier R. Molecular dynamics of apo-adenylate kinase: a principal component analysis. J Phys Chem B. 2006;110:12796-808 pubmed
    ..A pair of residues is suggested for labeling that would be useful for monitoring distance fluctuations by energy transfer experiments. ..
  26. Reinstein J, Schlichting I, Wittinghofer A. Structurally and catalytically important residues in the phosphate binding loop of adenylate kinase of Escherichia coli. Biochemistry. 1990;29:7451-9 pubmed
    ..The results obtained with K13Q suggest that this lysine residue, which is conserved in all guanine and many adenine nucleotide proteins, might have an important role in catalysis. ..
  27. Feng Y, Yang L, Kloczkowski A, Jernigan R. The energy profiles of atomic conformational transition intermediates of adenylate kinase. Proteins. 2009;77:551-8 pubmed publisher
    ..1998;11:739-747) and the k-means clustering algorithm are then used to show that known PDB structures closely resemble computed intermediates along the transition pathway. ..
  28. Orevi T, Ben Ishay E, Gershanov S, Dalak M, Amir D, Haas E. Fast closure of N-terminal long loops but slow formation of ? strands precedes the folding transition state of Escherichia coli adenylate kinase. Biochemistry. 2014;53:3169-78 pubmed publisher
    ..The study of subdomain folding in situ suggests a hierarchic ordered folding mechanism, in which early and rapid cross-linking by hydrophobic loop closure provides structural stabilization at the initiation of the folding pathway. ..
  29. Onuk E, Badger J, Wang Y, Bardhan J, Chishti Y, Akcakaya M, et al. Effects of Catalytic Action and Ligand Binding on Conformational Ensembles of Adenylate Kinase. Biochemistry. 2017;56:4559-4567 pubmed publisher
    Crystal structures of adenylate kinase (AdK) from Escherichia coli capture two states: an "open" conformation (apo) obtained in the absence of ligands and a "closed" conformation in which ligands are bound...
  30. Kim J, Shen R, Olcott M, Rajagopal I, Mathews C. Adenylate kinase of Escherichia coli, a component of the phage T4 dNTP synthetase complex. J Biol Chem. 2005;280:28221-9 pubmed
  31. Orevi T, Ben Ishay E, Pirchi M, Jacob M, Amir D, Haas E. Early closure of a long loop in the refolding of adenylate kinase: a possible key role of non-local interactions in the initial folding steps. J Mol Biol. 2009;385:1230-42 pubmed publisher
    ..We conclude that a specific network of non-local interactions, the closure of one or several loops, can play an important role in determining the protein folding pathway at its early phases. ..
  32. Lin Y, Nageswara Rao B. Structural characterization of adenine nucleotides bound to Escherichia coli adenylate kinase. 2. 31P and 13C relaxation measurements in the presence of cobalt(II) and manganese(II). Biochemistry. 2000;39:3647-55 pubmed
    ..These conformations differ significantly from the nucleotide conformations in crystals of AKe. AP(5)A and AKe.AMP.AMPPNP as determined by X-ray crystallography. ..
  33. Cukier R. Apo adenylate kinase encodes its holo form: a principal component and varimax analysis. J Phys Chem B. 2009;113:1662-72 pubmed publisher
    ..In this sense, apo AKE does encode in its fluctuations information about holo-like conformations. ..
  34. Blinkowa A, Gawecka G. Mechanism of conjugation. II. Characterization of an Hfr dna ts mutant of Escherichia coli K-12. Mol Gen Genet. 1979;172:107-11 pubmed
    ..coli chromosome. Upon temperature shift to 42 degrees C the DNA synthesis and transfer of chromosome is stopped immediately and RNA, protein synthesis in about ten minutes. ..
  35. Bock Möbius I, Brune M, Wittinghofer A, Zimmermann H, Leberman R, Dauvergne M, et al. Identification of valine/leucine/isoleucine and threonine/alanine/glycine proton-spin systems of Escherichia coli adenylate kinase by selective deuteration and selective protonation. Biochem J. 1991;273(Pt 2):311-6 pubmed
    ..Use of these proteins enabled identification of the spin systems of these amino acid residues in the n.m.r. spectra of the protein. ..
  36. Glushka J, Barzu O, Sarfati R, Kansal V, Cowburn D. The binding of ATP and AMP to Escherichia coli adenylate kinase investigated by 1H and 15N NMR spectroscopy. Biochem Biophys Res Commun. 1990;172:432-8 pubmed
  37. Skoblov J, Frank Kamenetskaya M, Chernov D, Krayevsky A. Modified nucleotides as substrates and inhibitors of adenylate kinase from different sources. FEBS Lett. 1996;395:283-5 pubmed
    ..3'-Azido-2',3'-dideoxythymidine and its phosphorus derivatives did not inhibit the adenylate kinase reaction. ..
  38. Reinstein J, Gilles A, Rose T, Wittinghofer A, Saint Girons I, Barzu O, et al. Structural and catalytic role of arginine 88 in Escherichia coli adenylate kinase as evidenced by chemical modification and site-directed mutagenesis. J Biol Chem. 1989;264:8107-12 pubmed
    ..It possibly stabilizes the transferable gamma-phosphate group from ATP to AMP in the transition state. ..
  39. Barzu O, Michelson S. Simple and fast purification of Escherichia coli adenylate kinase. FEBS Lett. 1983;153:280-4 pubmed
    ..1 microM in the case of mutant enzyme). After denaturation in 6 M guanidinium hydrochloride both mutant and parent adenylate kinase returned rapidly to the native, active state by dilution of guanidinium hydrochloride. ..
  40. Liang P, Glaser M. Efficient cloning of a mutant adenylate-kinase-encoding gene from Escherichia coli. Gene. 1989;80:21-8 pubmed
    ..A 15% frequency of homogenotization was obtained during cloning of an adk gene that encodes a temperature-sensitive adenylate kinase (AK)...
  41. Henson J, Blinkowa A, Walker J. The Escherichia coli dnaW mutation is an allele of the adk gene. Mol Gen Genet. 1982;186:488-92 pubmed
    A dnaW mutant, isolated on the basis of inability to effect conjugal DNA transfer at high temperature, has been shown by complementation and enzyme assay to be defective in the adk (adenylate kinase; EC 2.7.4.3) locus...
  42. Henzler Wildman K, Kern D. Dynamic personalities of proteins. Nature. 2007;450:964-72 pubmed
    ..This requires addition of a fourth dimension, time, to structural biology so that the positions in space and time of all atoms in a protein can be described in detail. ..
  43. Althoff S, Zambrowicz B, Liang P, Glaser M, Phillips G. Crystallization and preliminary X-ray analysis of Escherichia coli adenylate kinase. J Mol Biol. 1988;199:665-6 pubmed
  44. Gilles A, Marliere P, Rose T, Sarfati R, Longin R, Meier A, et al. Conservative replacement of methionine by norleucine in Escherichia coli adenylate kinase. J Biol Chem. 1988;263:8204-9 pubmed
    ..Bacteria, transformed by recombinant plasmid pIPD37 carrying the adk gene and grown under limiting methionine and excess norleucine, synthesize 16-20% of adenylate kinase molecules ..
  45. Gilles A, Saint Girons I, Monnot M, Fermandjian S, Michelson S, Barzu O. Substitution of a serine residue for proline-87 reduces catalytic activity and increases susceptibility to proteolysis of Escherichia coli adenylate kinase. Proc Natl Acad Sci U S A. 1986;83:5798-802 pubmed
    ..This seems to indicate that the "loosening" of the three-dimensional structure of E. coli adenylate kinase by proline----serine substitution is largely compensated for when an enzyme X ATP or enzyme X Ap5A complex is formed. ..
  46. Glaser M, Nulty W, Vagelos P. Role of adenylate kinase in the regulation of macromolecular biosynthesis in a putative mutant of Escherichia coli defective in membrane phospholipid biosynthesis. J Bacteriol. 1975;123:128-36 pubmed
    ..Adenylate kinase, therefore, is a key enzyme in controlling the rate of cell growth. The nature of the possible relationship between adenylate kinase and glycerol-3-phosphate acyltransferase is discussed. ..
  47. Schrank T, Bolen D, Hilser V. Rational modulation of conformational fluctuations in adenylate kinase reveals a local unfolding mechanism for allostery and functional adaptation in proteins. Proc Natl Acad Sci U S A. 2009;106:16984-9 pubmed publisher
    ..These findings open new avenues for rational protein design and fundamentally illuminate the role of local unfolding in function and adaptation. ..
  48. Shapiro Y, Kahana E, Meirovitch E. Domain mobility in proteins from NMR/SRLS. J Phys Chem B. 2009;113:12050-60 pubmed publisher
    ..94; the main ordering axis, Z(M), lies along N-H, <c(2)(0)> approximately = 16 (c(2)(2) = 0); and the slow local motional correlation time lies at the low end of the nanosecond time scale. ..
  49. Elamrani S, Berry M, Phillips G, McCammon J. Study of global motions in proteins by weighted masses molecular dynamics: adenylate kinase as a test case. Proteins. 1996;25:79-88 pubmed
    ..The end product of the simulation is similar to the known open and AMP bound forms of the enzyme. The biological relevance of the restraints used and potential methods of improving the technique are discussed. ..
  50. Tugarinov V, Shapiro Y, Liang Z, Freed J, Meirovitch E. A novel view of domain flexibility in E. coli adenylate kinase based on structural mode-coupling (15)N NMR relaxation. J Mol Biol. 2002;315:155-70 pubmed
    ..A powerful new model of protein flexibility/domain motion has been established. Conformational exchange (R(ex)) processes accompany the tau( perpendicular) mode. The SRLS analysis is compared with the conventional model-free analysis. ..
  51. Bilderback T, Fulmer T, Mantulin W, Glaser M. Substrate binding causes movement in the ATP binding domain of Escherichia coli adenylate kinase. Biochemistry. 1996;35:6100-6 pubmed
    ..These results suggest that there is significant closure of the ATP binding domain upon the binding of ATP or AP5A. Unexpectedly, exposure of the enzyme to AMP also introduced a partial closure of the ATP hinged domain. ..
  52. Perrier V, Burlacu Miron S, Bourgeois S, Surewicz W, Gilles A. Genetically engineered zinc-chelating adenylate kinase from Escherichia coli with enhanced thermal stability. J Biol Chem. 1998;273:19097-101 pubmed
    ..Moreover, the quadruple mutant exhibited a remarkably high thermal stability as compared with the wild-type form with preservation of the kinetic parameters of the parent enzyme. ..
  53. Cousin D, Buttin G. [Thermosensitive mutants of K12 Escherichia coli. 3. A lethal mutation of E. coli affecting the activity of the adenylate kinase]. Ann Inst Pasteur (Paris). 1969;117:612-30 pubmed
  54. Kern P, Brunne R, Folkers G. Nucleotide-binding properties of adenylate kinase from Escherichia coli: a molecular dynamics study in aqueous and vacuum environments. J Comput Aided Mol Des. 1994;8:367-88 pubmed
    ..Reliable results were achieved only if water was explicitly included in the stimulation. ..
  55. Bardwell J, Craig E. Eukaryotic Mr 83,000 heat shock protein has a homologue in Escherichia coli. Proc Natl Acad Sci U S A. 1987;84:5177-81 pubmed
    ..The gene encoding C62.5 (named htpG) is located between the dnaZ and adk genes at 11.1 minutes on the E. coli chromosome. The htpG gene appears to be a newly identified locus...
  56. Miyamoto K, Nakahigashi K, Nishimura K, Inokuchi H. Isolation and characterization of visible light-sensitive mutants of Escherichia coli K12. J Mol Biol. 1991;219:393-8 pubmed
    ..A possible mechanism for the killing of the visA mutant bacteria is discussed. ..
  57. Lu Q, Inouye M. Adenylate kinase complements nucleoside diphosphate kinase deficiency in nucleotide metabolism. Proc Natl Acad Sci U S A. 1996;93:5720-5 pubmed
    ..Among the nucleoside monophosphate kinases tested, only adenylate kinase was found to have NDP kinase activity. To our knowledge, this is the first report of NDP kinase activity associated with adenylate kinase. ..
  58. Sinev M, Landsmann P, Sineva E, Ittah V, Haas E. Design consideration and probes for fluorescence resonance energy transfer studies. Bioconjug Chem. 2000;11:352-62 pubmed
    ..General considerations for design of charged probes and site-directed labeling for applications of FRET methods in studies of protein structure and dynamics are presented. ..
  59. Rundqvist L, Adén J, Sparrman T, Wallgren M, Olsson U, Wolf Watz M. Noncooperative folding of subdomains in adenylate kinase. Biochemistry. 2009;48:1911-27 pubmed publisher
    ..Adenylate kinase (Adk) is composed of three subdomains: CORE, ATPlid, and AMPbd...
  60. Esmon B, Kensil C, Cheng C, Glaser M. Genetic analysis of Escherichia coli mutants defective in adenylate kinase and sn-glycerol 3-phosphate acyltransferase. J Bacteriol. 1980;141:405-8 pubmed
    ..The results suggest that the adk (plsA) locus is the structural gene for adenylate kinase.
  61. Reinstein J, Brune M, Wittinghofer A. Mutations in the nucleotide binding loop of adenylate kinase of Escherichia coli. Biochemistry. 1988;27:4712-20 pubmed
    The adk gene of Escherichia coli has been used to overexpress the adenylate kinase protein in two ways: (1) by cloning the adk gene with its own promoter into pEMBL plasmids, which have an increased copy number, and (2) by deleting the ..
  62. Ratner V, Amir D, Kahana E, Haas E. Fast collapse but slow formation of secondary structure elements in the refolding transition of E. coli adenylate kinase. J Mol Biol. 2005;352:683-99 pubmed
    ..The AK molecules undergo fast collapse to an ensemble of compact structures where the local environment of surface probes seems to be native-like but the two labeled secondary structure elements remain unfolded. ..
  63. Ittah V, Kahana E, Amir D, Haas E. Applications of time-resolved resonance energy transfer measurements in studies of the molecular crowding effect. J Mol Recognit. 2004;17:448-55 pubmed
    ..Networks of pairs of labeled sites can be prepared and tr-RET experiments can be performed in order to search for the segments of the protein molecules, which respond to the presence of inert macromolecules in their environment. ..
  64. Muller C, Schulz G. Structure of the complex of adenylate kinase from Escherichia coli with the inhibitor P1,P5-di(adenosine-5'-)pentaphosphate. J Mol Biol. 1988;202:909-12 pubmed
    ..The final R-factor is 35.9%. The corresponding model is given as backbone tracing. The structure will be used for protein-engineering studies. ..
  65. Reinstein J, Vetter I, Schlichting I, Rosch P, Wittinghofer A, Goody R. Fluorescence and NMR investigations on the ligand binding properties of adenylate kinases. Biochemistry. 1990;29:7440-50 pubmed
    ..coli (AKec) and 36 of AK1 are situated in a comparable environment and are not essential for catalytic activity. ..
  66. Saint Girons I, Gilles A, Margarita D, Michelson S, Monnot M, Fermandjian S, et al. Structural and catalytic characteristics of Escherichia coli adenylate kinase. J Biol Chem. 1987;262:622-9 pubmed
    The adk gene encoding adenylate kinase in Escherichia coli was cloned in pBR322. Adenylate kinase represented about 4% of total proteins in extracts of cells containing the pBR322:adk plasmid...
  67. Hershey H, Taylor M. Nucleotide sequence and deduced amino acid sequence of Escherichia coli adenine phosphoribosyltransferase and comparison with other analogous enzymes. Gene. 1986;43:287-93 pubmed
    ..All PRTs, including E. coli adenine PRT (APRT), have a strongly conserved 13-aa sequence, as well as other regions of aa sequence or structural similarity. E. coli APRT is remarkably similar to the mouse enzyme. ..
  68. Burlacu Miron S, Perrier V, Gilles A, Pistotnik E, Craescu C. Structural and energetic factors of the increased thermal stability in a genetically engineered Escherichia coli adenylate kinase. J Biol Chem. 1998;273:19102-7 pubmed
    ..In contrast, the Gibbs free energy of unfolding (at physiologically relevant conditions) of the quadruple mutant is lower than that of the wild type. ..
  69. Gigliobianco T, Lakaye B, Makarchikov A, Wins P, Bettendorff L. Adenylate kinase-independent thiamine triphosphate accumulation under severe energy stress in Escherichia coli. BMC Microbiol. 2008;8:16 pubmed publisher
    ..Furthermore, they show that E. coli accumulate large amounts of ThTP under severe energy stress when ATP levels are very low, an observation not in favor of an ATP-dependent mechanisms for ThTP synthesis. ..
  70. Arrondo J, Gilles A, Barzu O, Fermandjian S, Yang P, Mantsch H. Investigation of adenylate kinase from Escherichia coli and its interaction with nucleotides by Fourier transform infrared spectroscopy. Biochem Cell Biol. 1989;67:327-31 pubmed
    ..The effect of protein denaturing agents and conditions (temperature, high pH, sodium dodecyl sulfate) on changes in the protein conformation as revealed by the conformation-sensitive amide I bands is discussed. ..
  71. Willemoes M, Kilstrup M. Nucleoside triphosphate synthesis catalysed by adenylate kinase is ADP dependent. Arch Biochem Biophys. 2005;444:195-9 pubmed
    Adenylate kinase (Adk) that catalyses the synthesis of ADP from ATP and AMP has also been shown to perform an ATP dependent phosphorylation of ribo- and deoxynucleoside diphosphates to their corresponding nucleoside triphosphate; ATP+(d)..
  72. Ben Ishay E, Rahamim G, Orevi T, Hazan G, Amir D, Haas E. Fast subdomain folding prior to the global refolding transition of E. coli adenylate kinase: a double kinetics study. J Mol Biol. 2012;423:613-23 pubmed publisher
    ..Further experiments on studying the kinetics of folding of selected structural elements in the protein will help determination of the driving force of this early folding event...