D Moras

Summary

Country: France

Publications

  1. ncbi request reprint Dimerization of Escherichia coli DNA-gyrase B provides a structural mechanism for activating the ATPase catalytic center
    L Brino
    Institut de Genetique et de Biologie Moleculaire et Cellulaire IGBMC, CNRS INSERM, Universite Louis Pasteur, BP 163, 1 rue Laurent Fries, 67404 Illkirch Cedex, France
    J Biol Chem 275:9468-75. 2000
  2. ncbi request reprint The nuclear receptor ligand-binding domain: structure and function
    D Moras
    Institut de Genetique et de Biologie Moleculaire et Cellulaire IGBMC, CNRS INSERM ULP, Illkirch, France
    Curr Opin Cell Biol 10:384-91. 1998
  3. ncbi request reprint Zinc ion mediated amino acid discrimination by threonyl-tRNA synthetase
    R Sankaranarayanan
    UPR 9004 Biologie Structurale, IGBMC, CNRS INSERM ULP, Illkirch, France
    Nat Struct Biol 7:461-5. 2000
  4. ncbi request reprint Transfer RNA-mediated editing in threonyl-tRNA synthetase. The class II solution to the double discrimination problem
    A Dock-Bregeon
    UPR 9004 Biologie Structurale IGBMC, CNRS INSERM ULP BP163 67404 Cedex, Illkirch, France
    Cell 103:877-84. 2000
  5. ncbi request reprint Dissecting the interaction network of multiprotein complexes by pairwise coexpression of subunits in E. coli
    S Fribourg
    , CNRS/INSERM/ULP, , BP 163, Cedex C.U. de Strasbourg, Illkirch, 67404, France
    J Mol Biol 306:363-73. 2001
  6. ncbi request reprint Glycyl-tRNA synthetase uses a negatively charged pit for specific recognition and activation of glycine
    J G Arnez
    Laboratoire de Biologie Structurale, Institut de Genetique et de Biologie Moleculaire et Cellulaire, CNRS INSERM ULP, Illkirch Cedex, 67404, France
    J Mol Biol 286:1449-59. 1999
  7. ncbi request reprint Aspartyl tRNA-synthetase from Escherichia coli: flexibility and adaptability to the substrates
    B Rees
    UPR 9004, Laboratoire de Biologie et de Génomique Structurales, Institut de Genetique et de Biologie Moleculaire et Cellulaire, 1 rue Laurent Fries, Illkirch, 67400, France
    J Mol Biol 299:1157-64. 2000
  8. pmc The human TFIID components TAF(II)135 and TAF(II)20 and the yeast SAGA components ADA1 and TAF(II)68 heterodimerize to form histone-like pairs
    Y G Gangloff
    Institut de Genetique et de Biologie Moleculaire et Cellulaire, CNRS INSERM ULP, Illkirch Cedex, C U de Strasbourg, France
    Mol Cell Biol 20:340-51. 2000
  9. pmc The structure of an AspRS-tRNA(Asp) complex reveals a tRNA-dependent control mechanism
    L Moulinier
    UPR 9004, Laboratoire de Biologie et Genomique Structurales, Institut de Genetique et de Biologie Moleculaire et Cellulaire, CNRS INSERM ULP, 1 rue Laurent Fries, BP 163, 67404 Illkirch Cedex, France
    EMBO J 20:5290-301. 2001
  10. pmc L-arginine recognition by yeast arginyl-tRNA synthetase
    J Cavarelli
    UPR 9004 Biologie Structurale, , CNRS INSERM ULP, BP 163, 67404 Illkirch Cedex, France
    EMBO J 17:5438-48. 1998

Collaborators

Detail Information

Publications50

  1. ncbi request reprint Dimerization of Escherichia coli DNA-gyrase B provides a structural mechanism for activating the ATPase catalytic center
    L Brino
    Institut de Genetique et de Biologie Moleculaire et Cellulaire IGBMC, CNRS INSERM, Universite Louis Pasteur, BP 163, 1 rue Laurent Fries, 67404 Illkirch Cedex, France
    J Biol Chem 275:9468-75. 2000
    ....
  2. ncbi request reprint The nuclear receptor ligand-binding domain: structure and function
    D Moras
    Institut de Genetique et de Biologie Moleculaire et Cellulaire IGBMC, CNRS INSERM ULP, Illkirch, France
    Curr Opin Cell Biol 10:384-91. 1998
    ..Recent data have provided the structural basis for the specific recognition of ligands and the molecular mechanisms of agonism and antagonism, enabling us to gain a comprehensive view of the early steps of nuclear receptor action...
  3. ncbi request reprint Zinc ion mediated amino acid discrimination by threonyl-tRNA synthetase
    R Sankaranarayanan
    UPR 9004 Biologie Structurale, IGBMC, CNRS INSERM ULP, Illkirch, France
    Nat Struct Biol 7:461-5. 2000
    ..This study demonstrates that the zinc ion is neither strictly catalytic nor structural and suggests how the zinc ion ensures that only amino acids that possess a hydroxyl group attached to the beta-position are activated...
  4. ncbi request reprint Transfer RNA-mediated editing in threonyl-tRNA synthetase. The class II solution to the double discrimination problem
    A Dock-Bregeon
    UPR 9004 Biologie Structurale IGBMC, CNRS INSERM ULP BP163 67404 Cedex, Illkirch, France
    Cell 103:877-84. 2000
    ..As a consequence, the editing mechanism of both classes of synthetases can be described as mirror images, as already seen for tRNA binding and amino acid activation...
  5. ncbi request reprint Dissecting the interaction network of multiprotein complexes by pairwise coexpression of subunits in E. coli
    S Fribourg
    , CNRS/INSERM/ULP, , BP 163, Cedex C.U. de Strasbourg, Illkirch, 67404, France
    J Mol Biol 306:363-73. 2001
    ..Coexpression can be used as an alternative or complementary approach to conventional techniques for interaction studies such as yeast two-hybrid analysis, GST pulldown and immunoprecipitation...
  6. ncbi request reprint Glycyl-tRNA synthetase uses a negatively charged pit for specific recognition and activation of glycine
    J G Arnez
    Laboratoire de Biologie Structurale, Institut de Genetique et de Biologie Moleculaire et Cellulaire, CNRS INSERM ULP, Illkirch Cedex, 67404, France
    J Mol Biol 286:1449-59. 1999
    ..On the basis of this similarity, we propose that GlyRS utilizes the same general mechanism as that employed by other class II aminoacyl-tRNA synthetases...
  7. ncbi request reprint Aspartyl tRNA-synthetase from Escherichia coli: flexibility and adaptability to the substrates
    B Rees
    UPR 9004, Laboratoire de Biologie et de Génomique Structurales, Institut de Genetique et de Biologie Moleculaire et Cellulaire, 1 rue Laurent Fries, Illkirch, 67400, France
    J Mol Biol 299:1157-64. 2000
    ..In contrast to these induced-fit conformational changes, a few residues essential for the tRNA anticodon or aspartyl-adenylate recognition exist in a predefined conformation, ensured by specific interactions within the protein...
  8. pmc The human TFIID components TAF(II)135 and TAF(II)20 and the yeast SAGA components ADA1 and TAF(II)68 heterodimerize to form histone-like pairs
    Y G Gangloff
    Institut de Genetique et de Biologie Moleculaire et Cellulaire, CNRS INSERM ULP, Illkirch Cedex, C U de Strasbourg, France
    Mol Cell Biol 20:340-51. 2000
    ..These results are indicative of a histone fold type of interaction between hTAF(II)20-hTAF(II)135 and yTAF(II)68-yADA1, which therefore constitute novel histone-like pairs in the TFIID and SAGA complexes...
  9. pmc The structure of an AspRS-tRNA(Asp) complex reveals a tRNA-dependent control mechanism
    L Moulinier
    UPR 9004, Laboratoire de Biologie et Genomique Structurales, Institut de Genetique et de Biologie Moleculaire et Cellulaire, CNRS INSERM ULP, 1 rue Laurent Fries, BP 163, 67404 Illkirch Cedex, France
    EMBO J 20:5290-301. 2001
    ..Solution and cellular studies on mutant tRNAs confirm the crucial role of the tRNA three-dimensional structure versus a specific recognition of bases in the control mechanism...
  10. pmc L-arginine recognition by yeast arginyl-tRNA synthetase
    J Cavarelli
    UPR 9004 Biologie Structurale, , CNRS INSERM ULP, BP 163, 67404 Illkirch Cedex, France
    EMBO J 17:5438-48. 1998
    ..This tyrosine is also conserved in other class I aaRS active sites but plays several functional roles. The ArgRS structure allows the definition of a new framework for sequence alignments and subclass definition in class I aaRSs...
  11. ncbi request reprint Molecular structure of human TFIIH
    P Schultz
    Institut de Génétique et de Biologie Moléclaire et Cellulaire, CNRS INSERM ULP, Illkirch, France
    Cell 102:599-607. 2000
    ..Within the ring structure, p44 was flanked on either side by the XPB and XPD helicases. These observations provide us with a quartenary organizational model of TFIIH...
  12. ncbi request reprint Structural characterization of the cysteine-rich domain of TFIIH p44 subunit
    S Fribourg
    Institut de Genetique et de Biologie Moleculaire et Cellulaire, CNRS INSERM ULP, 1, rue Laurent Fries, Boite Postale 163, 67404 Illkirch Cedex, France
    J Biol Chem 275:31963-71. 2000
    ..The solution structure of this second module reveals an unexpected homology with the regulatory domain of protein kinase C and provides a framework to study its role at the molecular level...
  13. ncbi request reprint The structure of Staphylococcus aureus epidermolytic toxin A, an atypic serine protease, at 1.7 A resolution
    J Cavarelli
    Institut de Genetique et de Biologie Moleculaire et Cellulaire, CNRS INSERM ULP, Illkirch, France
    Structure 5:813-24. 1997
    ..Determination of the structure of ETA and its comparison with other serine proteases may reveal insights into ETA's catalytic mechanism...
  14. ncbi request reprint Crystallization of threonyl-tRNA synthetase from Thermus thermophilus and preliminary crystallographic data
    V Cura
    UPR 9004 de Biologie Structurale, IGBMC, CNRS INSERM ULP, Illkirch, France
    FEBS Lett 374:110-2. 1995
    ..This paper reports the first crystals of ttTRS and preliminary crystallographic results since the presumed crystals of ttTRS described in a previous paper [1] were crystals of aspartyl-tRNA synthetase [2]...
  15. ncbi request reprint Overexpression, purification, and crystal structure of native ER alpha LBD
    S Eiler
    Laboratoire de Biologie et Génomique Structurales 1, IGBMC, rue Laurent Fries, Illkirch, 67404, France
    Protein Expr Purif 22:165-73. 2001
    ..The present strategy can be adapted to other cases where the solubility and the proper folding is a difficulty...
  16. ncbi request reprint Crystallization of the 43 kDa ATPase domain of Thermus thermophilus gyrase B in complex with novobiocin
    V Lamour
    Institut de Génétique et de Biologie Moléculaire, CNRS INSERM ULP, BP 10142, 1 rue Laurent Fries, 67404 Illkirch Cedex, France
    Acta Crystallogr D Biol Crystallogr 58:1376-8. 2002
    ..3 A allowing the determination of the first structure of a gyrase B 43K domain in complex with a coumarin...
  17. pmc tRNA aminoacylation by arginyl-tRNA synthetase: induced conformations during substrates binding
    B Delagoutte
    UPR 9004 Biologie et Génomique Structurales, Institut de Genetique et de Biologie Moleculaire et Cellulaire, CNRS INSERM ULP, BP 163, 67404 Illkirch Cedex, France
    EMBO J 19:5599-610. 2000
    ..Several key residues of the active site play multiple roles in the catalytic pathway and thus highlight the structural dynamics of the aminoacylation reaction...
  18. pmc Synthesis of aspartyl-tRNA(Asp) in Escherichia coli--a snapshot of the second step
    S Eiler
    UPR 9004, Laboratoire de Biologie Structurale, Institut de Genetique et de Biologie Moleculaire et Cellulaire, CNRS INSERM ULP, 1 rue Laurent Fries, BP 163, 67404 Illkirch Cedex, C U de Strasbourg, France
    EMBO J 18:6532-41. 1999
    ....
  19. ncbi request reprint The TBP-like factor: an alternative transcription factor in metazoa?
    J C Dantonel
    Institut de Genetique et de Biologie Moleculaire et Cellulaire, CNRS INSERM ULP, BP 163, F 67404 Illkirch, Cedex, C U de Strasbourg, France
    Trends Biochem Sci 24:335-9. 1999
    ..Thus, the existence of TLFs presents a challenge to the doctrine that TBP is a universal regulator of transcription in metazoans...
  20. ncbi request reprint The crystal structure of the nuclear receptor for vitamin D bound to its natural ligand
    N Rochel
    Laboratoire de Biologie Structurale, Institut de Genetique et de Biologie Moleculaire et Cellulaire CNRS INSERM ULP, Illkirch, France
    Mol Cell 5:173-9. 2000
    ..The structure reveals the active conformation of the bound ligand and allows understanding of the different binding properties of some synthetic analogs...
  21. ncbi request reprint Crystallization and preliminary X-ray crystallographic analysis of yeast arginyl-tRNA synthetase-yeast tRNAArg complexes
    B Delagoutte
    UPR 9004 Biologie Structurale, , CNRS INSERM ULP, BP 163, 67404 Illkirch Cedex, France
    Acta Crystallogr D Biol Crystallogr 56:492-4. 2000
    ..The estimated V(m) of 2.6 A(3) Da(-1) indicates one molecule of complex in the asymmetric unit. The three crystal forms were solved by the molecular-replacement method using the coordinates of the free yArgRS...
  22. ncbi request reprint The fidelity of the translation of the genetic code
    R Sankaranarayanan
    Laboratoire de Biologie et Genomique Structurales, IGBMC, CNRS INSERM ULP, Illkirch, Strasbourg, France
    Acta Biochim Pol 48:323-35. 2001
    ..These studies led us to propose a model which emphasizes the mirror symmetrical approach of the two classes of enzymes and highlights that tRNA is the key player in the evolution of these class of enzymes...
  23. ncbi request reprint Ultrahigh resolution drug design I: details of interactions in human aldose reductase-inhibitor complex at 0.66 A
    E I Howard
    Laboratoire de Génomique et de Biologie Structurales, UMR 7104 du CNRS, IGBMC, Illkirch, France
    Proteins 55:792-804. 2004
    ..This work demonstrates the capabilities of subatomic resolution experiments and stimulates further developments of methods allowing the use of the full potential of these experiments...
  24. ncbi request reprint Sequence analysis and modular organization of threonyl-tRNA synthetase from Thermus thermophilus and its interrelation with threonyl-tRNA synthetases of other origins
    V Cura
    UPR 9004 du CNRS, Institut de Genetique et de Biologie Moleculaire et Cellulaire, Illkirch, France
    Eur J Biochem 267:379-93. 2000
    ..coli thrS and Bacillus subtilis thrS and thrZ. Here we discuss our results in the context of evolution of the threonylation systems and of the position of T. thermophilus in the phylogenic tree...
  25. pmc A new model for 20-hydroxyecdysone and dibenzoylhydrazine binding: a homology modeling and docking approach
    J M Wurtz
    Laboratoire de Biologie Structurale, Institut de Genetique et de Biologie Moleculaire et Cellulaire, CNRS INSERM ULP, Illkirch, C U de Strasbourg, France
    Protein Sci 9:1073-84. 2000
    ..The homology model complexes provide new insights that can be exploited in the rational design of new environmentally safe insecticides...
  26. ncbi request reprint The structure of threonyl-tRNA synthetase-tRNA(Thr) complex enlightens its repressor activity and reveals an essential zinc ion in the active site
    R Sankaranarayanan
    UPR 9004 Biologie Structurale, Institut de Genetique et de Biologie Moleculaire et Cellulaire, CNRS INSERM ULP, Illkirch, France
    Cell 97:371-81. 1999
    ..A zinc ion found in the active site is implicated in amino acid recognition/discrimination...
  27. pmc Crystal structure of glycyl-tRNA synthetase from Thermus thermophilus
    D T Logan
    Institut de Genetique et de Biologie Moleculaire et Cellulaire, CNRS INSERM ULP, BP 163, Illkirch, France
    EMBO J 14:4156-67. 1995
    ..The active site residues most probably responsible for substrate recognition, in particular in the Gly binding pocket, can be identified by inference from aspartyl-tRNA synthetase due to the conserved nature of the class II active site...
  28. pmc Estrogen receptor transcription and transactivation: Structure-function relationship in DNA- and ligand-binding domains of estrogen receptors
    M Ruff
    IGBMC, UPR de biologie et génomique structurale, 1 rue Laurent Fries, 67404 Illkirch, France
    Breast Cancer Res 2:353-9. 2000
    ....
  29. pmc Crystal structure of histidyl-tRNA synthetase from Escherichia coli complexed with histidyl-adenylate
    J G Arnez
    INSERM ULP BP 163, Illkirch, France
    EMBO J 14:4143-55. 1995
    ..The modular domain organization of histidyl-tRNA synthetase reiterates a repeated theme in aaRS, and its structure should provide insight into the ability of certain aaRS to aminoacylate minihelices and other non-tRNA molecules...
  30. pmc Crystal structure of aspartyl-tRNA synthetase from Pyrococcus kodakaraensis KOD: archaeon specificity and catalytic mechanism of adenylate formation
    E Schmitt
    Laboratoire de Biologie Structurale, Institut de Genetique et de Biologie Moleculaire et Cellulaire, CNRS INSERM ULP, 1 rue Laurent Fries, BP163, 67404 Illkirch Cedex, C U de Strasbourg, France
    EMBO J 17:5227-37. 1998
    ..An unambiguous spatial and functional assignment of three magnesium ion cofactors can be made. This study shows the important role of residues present in both archaeal and eukaryotic AspRSs, but absent from the eubacterial enzymes...
  31. ncbi request reprint Human TAF(II)28 and TAF(II)18 interact through a histone fold encoded by atypical evolutionary conserved motifs also found in the SPT3 family
    C Birck
    Institut de Genetique et de Biologie, Moleculaire et Cellulaire, CNRS INSERM ULP, Illkirch, C U de Strasbourg, France
    Cell 94:239-49. 1998
    ..The existence of additional histone-like pairs in both the TFIID and SAGA complexes shows that the histone fold is a more commonly used motif for mediating TAF-TAF interactions than previously believed...
  32. ncbi request reprint Conformational adaptation of agonists to the human nuclear receptor RAR gamma
    B P Klaholz
    Institut de Genetique et de Biologie Moleculaire et Cellulaire, Universite Louis Pasteur, Illkirch, France
    Nat Struct Biol 5:199-202. 1998
  33. ncbi request reprint A 'specificity' pocket inferred from the crystal structures of the complexes of aldose reductase with the pharmaceutically important inhibitors tolrestat and sorbinil
    A Urzhumtsev
    UPR de Biologie Structurale 9004 IGMBC CNRS INSERM ULP 1 rue Laurent Fries, B P 163, 67404, Illkirch, France
    Structure 5:601-12. 1997
    ..The inhibitor zopolrestat binds to this anionic site, and in the hydrophobic cleft, after a change of conformation which opens a 'specificity' pocket...
  34. pmc Crystal structure of a prokaryotic aspartyl tRNA-synthetase
    M Delarue
    Laboratoire de Biologie Structurale, IBMC du CNRS, Strasbourg, France
    EMBO J 13:3219-29. 1994
    ..The T. thermophilus enzyme exhibits some features not found in any of the six other known AspRSs from mesophilic organisms...
  35. ncbi request reprint Crystal structure of a mutant hERalpha ligand-binding domain reveals key structural features for the mechanism of partial agonism
    M Gangloff
    Institut de Genetique et de Biologie Moleculaire et Cellulaire, , rue Laurent Fries, BP 163 67404 Illkirch, France
    J Biol Chem 276:15059-65. 2001
    ..These observations support a dynamic view of H12 positioning, where the control of the equilibrium between two stable locations determines the partial agonist character of a given ligand...
  36. ncbi request reprint Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha
    W Bourguet
    Institut de Genetique et de Biologie Moleculaire et Cellulaire, CNRS INSERM ULP College de France, Illkirch, CU de Strasbourg
    Nature 375:377-82. 1995
    ..Several lines of evidence indicate that the overall structure is a prototype fold of ligand-binding domains of nuclear receptors...
  37. ncbi request reprint Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs
    G Eriani
    Laboratoires de Biochimie, IBMC du CNRS, Strasbourg, France
    Nature 347:203-6. 1990
    ..Surprisingly, this partition of aaRS in two classes is found to be strongly correlated on the functional level with the acylation occurring either on the 2' OH (class I) or 3' OH (class II) of the ribose of the last nucleotide of tRNA...
  38. ncbi request reprint Rapid purification of the Aeromonas proteolytica aminopeptidase: crystallization and preliminary X-ray data
    C Schalk
    Marion Merrell Dow Research Institute, Strasbourg, France
    Arch Biochem Biophys 294:91-7. 1992
    ..1 A and c = 97.8 A. Assuming one molecule/asymmetric unit, a value of VM = 2.6 A3/Da and an approximate solvent content of 45% could be estimated. Measurable diffraction intensities were observed at a resolution of 2.5 A...
  39. ncbi request reprint Synthesis and recognition of aspartyl-adenylate by Thermus thermophilus aspartyl-tRNA synthetase
    A Poterszman
    Laboratoire de Biologie Structurale, I B M C du C N R S, Strasbourg, France
    J Mol Biol 244:158-67. 1994
    ..Conformational changes have been identified which allow the description of a reaction pathway including both lock-and-key and induced-fit interactions. This pathway can presumably be extended to all class II aaRS...
  40. ncbi request reprint Crystallization of E. coli aspartate beta-semialdehyde dehydrogenase
    J C Thierry
    Biochimie 62:739-40. 1980
  41. ncbi request reprint Crystallization of histidyl-tRNA synthetase from Escherichia coli
    C Francklyn
    Department of Biochemistry, University of Vermont College of Medicine, Burlington 05405
    J Mol Biol 241:275-7. 1994
    ..4 A3/dalton, the asymmetric unit in both forms contains two dimers with a solvent content of approximately 60%. A 3.7 A resolution native dataset with an Rmerge on intensities of 7.9% has been collected from the monoclinic crystal form...
  42. ncbi request reprint The 2.0 A crystal structure of Thermus thermophilus methionyl-tRNA synthetase reveals two RNA-binding modules
    I Sugiura
    Department of Chemistry, Faculty of Science, Ochanomizu University, Otsuka, Bunkyo ku, 112 8610, Japan
    Structure 8:197-208. 2000
    ..The class I synthetases are further divided into three subclasses, a, b and c, according to sequence homology. No conserved structural features for tRNA recognition by class I synthetases have been established...
  43. pmc The first step of aminoacylation at the atomic level in histidyl-tRNA synthetase
    J G Arnez
    Institut de Genetique et de Biologie Moleculaire et Cellulaire, Centre National de la Recherche Scientifique Institut National de la Santé et de la Recherche Médicale Université Louis Pasteur, BP 163, 67404 Strasbourg Illkirch, Cedex, France
    Proc Natl Acad Sci U S A 94:7144-9. 1997
    ..The use of both conserved metal ions and arginine in phosphoryl transfer provides evidence of significant early functional divergence of class II aminoacyl-tRNA synthetases...
  44. pmc Characterization of a thermosensitive Escherichia coli aspartyl-tRNA synthetase mutant
    F Martin
    UPR 9002, Structure des Macromolecules Biologiques et Mecanismes de Reconnaissance, CNRS, Institut de Biologie Moleculaire et Cellulaire, Strasbourg, France
    J Bacteriol 179:3691-6. 1997
    ....
  45. ncbi request reprint An intermediate step in the recognition of tRNA(Asp) by aspartyl-tRNA synthetase
    C Briand
    IGBMC CNRS INSERM ULP, UPR 9004, Laboratoire de Biologie et Génomique Structurale, 1, rue Laurent Fries, Illkirch Cedex, C U de Strasbourg, B P 163, France
    J Mol Biol 299:1051-60. 2000
    ..Based on these data, a pathway for tRNA binding and recognition is proposed...
  46. ncbi request reprint Crystallization and preliminary X-ray analysis of Escherichia coli methionyl-tRNA(fMet) formyltransferase
    E Schmitt
    Laboratorie de Biochimie, Unité de Recherche Associëe no 1970 du Centre National de la Recherche Scientifique, Ecole Polytechnique, Palaiseau, France
    Proteins 25:139-41. 1996
    ..The crystals are trigonal and have unit cell parameters a = b = 151.0 A, c = 81.8 A. They belong to space group P3(2)21 and diffract to 2.0 A resolution. The structure is being solved by multiple isomorphous replacement...
  47. ncbi request reprint Sequence, overproduction and crystallization of aspartyl-tRNA synthetase from Thermus thermophilus. Implications for the structure of prokaryotic aspartyl-tRNA synthetases
    A Poterszman
    Laboratoire de Biochimie, URA 240 CNRS, Ecole Polytechnique, Palaiseau, France
    FEBS Lett 325:183-6. 1993
    ..2 A resolution (space group P2(1)2(1)2(1), a = 61.4 A, b = 156.1 A, c = 177.3 A) are routinely obtained. The same crystals have previously been described as crystals of threonyl-tRNA synthetase [1]...
  48. ncbi request reprint Overproduction and purification of native and queuine-lacking Escherichia coli tRNA(Asp). Role of the wobble base in tRNA(Asp) acylation
    F Martin
    Institut de Biologie Moleculaire et Cellulaire du Centre National de la Recherche Scientifique, Strasbourg, France
    J Mol Biol 234:965-74. 1993
    ..coli, where only one contact is thought to occur at position 34...
  49. ncbi request reprint Crystallisation of the glycyl-tRNA synthetase from Thermus thermophilus and initial crystallographic data
    D T Logan
    UPR de Biologie Structurale, Strasbourg, France
    J Mol Biol 241:732-5. 1994
    ..The best native data extend to 2.9 A in C2,2,2(1) and are 90.6% complete with an R-factor between symmetry-related reflections of 10.0%. The structure has been solved by multiple isomorphous replacement and model building is in progress...
  50. ncbi request reprint Crystal structure of the stromelysin-3 (MMP-11) catalytic domain complexed with a phosphinic inhibitor mimicking the transition-state
    A L Gall
    Structural Biology and Genomics Laboratory, I G B M C, B P 163, F67404, Illkirch Cedex, France
    J Mol Biol 307:577-86. 2001
    ..Our crystal structure provides a good model to study the MMPs mechanism of proteolysis...