Crystal Structures of Weissella viridescens FemX and Its Complex with UDP-MurNAc-Pentapeptide: Insights into FemABX Family Substrates Recognition

Structure

Volumn 12, Issue 2, 2004, Pages 257-267

  Biarrotte Sorin, Sabrina ^a   Maillard, Antoine P ^b   Delettré, Jean ^a   Sougakoff, Wladimir ^c   Arthur, Michel ^b   Mayer, Claudine ^a  

^a UNIVERSITÉ PIERRE ET MARIE CURIE   (France)

^b SORBONNE UNIVERSITÉ   (France)

^c PITIÉ SALPÊTRIÈRE HOSPITAL   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ACYLTRANSFERASE; ALANINE; ALANINE TRANSFERASE FEMX; FEMABX PROTEIN; MURAMIC ACID; N ACETYLMURAMIC ACID; PENTAPEPTIDE; PROTEIN DERIVATIVE; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR GCN5; TRANSFER RNA; TRANSFERASE; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE;

AMINO ACID SEQUENCE; AMINOACYLATION; ARTICLE; BINDING SITE; COMPLEX FORMATION; CONTROLLED STUDY; CORRELATION ANALYSIS; CRYSTAL STRUCTURE; EVOLUTION; GRAM POSITIVE BACTERIUM; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; STRUCTURE ANALYSIS; WEISELLA VIRIDESCENS;

BACTERIA (MICROORGANISMS); POSIBACTERIA; WEISELLA; WEISSELLA VIRIDESCENS;

EID: 1242283845     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(04)00009-7     Document Type: Article

References (35)

1. Benson T.E., Prince D., Mutchler V., Curry K., Ho A., Sarver R., Hagadorn J., Choi G., Garlick R. X-ray crystal structure of Staphylococcus aureus FemA. Structure (Camb.). 10:2002;1107-1115.
2. Biarrotte-Sorin S., Maillard A.P., Delettre J., Sougakoff W., Blanot D., Blondeau K., Hugonnet J.-E., Mayer C., Arthur M. Crystallization and preliminary X-ray analysis of Weissella viridescens FemX UDP-MurNAc- pentapeptide:l-alanine ligase. Acta Crystallogr. D. 59:2003;1055-1057.
3. Biou V., Yaremchuk A., Tukalo M., Cusack S. The 2.9 Å crystal structure of T. thermophilus seryl-tRNA synthetase complexed with tRNA(Ser). Science. 263:1994;1404-1410.
4. Bouhss A., Josseaume N., Allanic D., Crouvoisier M., Gutmann L., Mainardi J.-L., Mengin-Lecreulx D., van Heijenoort J., Arthur M. Identification of the UDP-MurNAc-pentapeptide:L-alanine ligase for synthesis of branched peptidoglycan precursors in Enterococcus faecalis. J. Bacteriol. 183:2001;5122-5127.
5. Bouhss A., Josseaume N., Severin A., Tabei K., Hugonnet J.E., Shlaes D., Mengin-Lecreulx D., Van Heijenoort J., Arthur M. Synthesis of the L-alanyl-L-alanine cross-bridge of Enterococcus faecalis peptidoglycan. J. Biol. Chem. 277:2002;45935-45941.
6. Brünger A.T., Adams P.D., Clore G.M., DeLano W.L., Gros P., Grosse-Kunstleve R.W., Jiang J.-S., Kuszewski J., Nilges M., Pannu N.S.et al. Crystallography and NMR system. a new software suite for macromolecular structure determination Acta Crystallogr. D. 54:1998;905-921.
7. CCP4 Collaborative Computational Project. 4)(Acta Crystallogr. D 50):1994;760-763.
8. DeLano W.L. The PyMOL Molecular Graphics System. 2002;DeLano Scientific, San Carlos, CA.
9. Dyda F., Klein D., Hickman A.B. GCN5-related N-acetyltransferases. a structural overview Annu. Rev. Biophys. Biomol. Struct. 29:2000;81-103.
10. Filipe S.R., Tomasz A. Inhibition of the expression of penicillin resistance in Streptococcus pneumoniae by inactivation of cell wall muropeptide branching genes. Proc. Natl. Acad. Sci. USA. 97:2000;4891-4896.
11. Filipe S.R., Severina E., Tomasz A. Functional analysis of Streptococcus pneumoniae MurM reveals the region responsible for its specificity in the synthesis of branched cell wall peptides. J. Biol. Chem. 276:2001;39618-39628.
12. Gibrat J.-F., Madej T., Bryant S.H. Surprising similarities in structure comparison. Curr. Opin. Struct. Biol. 6:1996;377-385.
13. Gordon E.J., Flouret B., Chantalat L., Van Heijenoort J., Mengin-Lecreulx D., Dideberg O. Crystal structure of UDP-N-acetylmuramoyl-L- alanyl-D-glutamate. meso-diaminopimelate ligase from Escherichia coli J. Biol. Chem. 276:2001;10999-11006.
14. He H., Ding Y., Bartlam M., Sun F., Le Y., Qin X., Tang H., Zhang R., Joachimiak A., Liu J.et al. Crystal structure of tabtoxin resistance protein complexed with acetyl coenzyme A reveals the mechanism for beta-lactam acetylation. J. Mol. Biol. 325:2003;1019-1030.
15. Hegde S.S., Shrader T.E. FemABX family members are novel nonribosomal peptidyltransferases and important pathogen-specific drug targets. J. Biol. Chem. 276:2001;6998-7003.
16. Jones T.A., Zou J.Y., Cowan S.W., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A. 47:1991;110-119.
17. Jung J., Lee B. Circularly permuted proteins in the protein structure database. Protein Sci. 10:2001;1881-1886.
18. Kleywegt G.J. Use of non-crystallographic symmetry in protein structure refinement. Acta Crystallogr. D. 52:1996;842-857.
19. Ladner J.E., Jack A., Robertus J.D., Brown R., Rhodes D., Clark B.F., Klug A. Structure of yeast phenylalanine transfer RNA at 2.5 Å resolution. Proc. Natl. Acad. Sci. USA. 72:1975;4414-4418.
20. Murzin A.G., Brenner S.E., Hubbard T., Chothia C. Scop. a structural classification of proteins database for the investigation of sequences and structures J. Mol. Biol. 247:1995;536-540.
21. Neuwald A.F., Landsman D. GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein. Trends Biochem. Sci. 22:1997;154-155.
22. Nicholls A., Sharp K.A., Honig B. Protein folding and association. insights from the interfacial and thermodynamic properties of hydrocarbons Proteins. 11:1991;281-296.
23. Nissen P., Kjeldgaard M., Thirup S., Polekhina G., Reshetnikova L., Clark B.F., Nyborg J. Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog. Science. 270:1995;1464-1472.
24. Perrakis A., Morris R., Lamzin V.S. Automated protein model building combined with iterative structure refinement. Nat. Struct. Biol. 6:1999;458-463.
25. Plapp R., Strominger J.L. Biosynthesis of the peptidoglycan of bacterial cell walls. 18. Purification and properties of L-alanyl transfer ribonucleic acid-uridine diphosphate-N-acetylmuramyl-pentapeptide transferase from Lactobacillus viridescens. J. Biol. Chem. 245:1970;3675-3682.
26. Plewniak F., Bianchetti L., Brelivet Y., Carles A., Chalmel F., Lecompte O., Mochel T., Moulinier L., Muller A., Muller J.et al. PipeAlign. a new toolkit for protein family analysis Nucleic Acids Res. 31:2003;3829-3832.
27. Powell H.R. The Rossmann Fourier autoindexing algorithm in MOSFLM. Acta Crystallogr. D. 55:1999;1690-1695.
28. Rohrer S., Berger-Bächi B. FemABX peptidyl transferases. a link between branched-chain cell wall peptide formation and beta-lactam resistance in gram-positive cocci Antimicrob. Agents Chemother. 47:2003;837-846.
29. Rohrer S., Ehlert K., Tschierske M., Labischinski H., Berger-Bächi B. The essential Staphylococcus aureus gene fmhB is involved in the first step of peptidoglycan pentaglycine interpeptide formation. Proc. Natl. Acad. Sci. USA. 96:1999;9351-9356.
30. Roth M., Carpentier P., Kaikati O., Joly J., Charrault P., Pirocchi M., Kahn R., Fanchon E., Jacquamet L., Borel F.et al. Fip. a highly automated beamline for multiwavelength anomalous diffraction experiments Acta Crystallogr. D. 58:2002;805-814.
31. Rould M.A., Perona J.J., Söll D., Steitz T.A. Structural basis for misaminoacylation by mutant E. coli glutaminyl-tRNA synthetase enzymes. Science. 246:1989;1135-1142.
32. Schleifer K.H., Kandler O. Peptidoglycan types of bacterial cell walls and their taxonomic implications. Bacteriol. Rev. 36:1972;407-477.
33. Schmitt E., Panvert M., Blanquet S., Mechulam Y. Crystal structure of methionyl-tRNAfMet transformylase complexed with the initiator formyl-methionyl-tRNAfMet. EMBO J. 17:1998;6819-6826.
34. Uliel S., Fliess A., Unger R. Naturally occurring circular permutations in proteins. Protein Eng. 14:2001;533-542.
35. Weston S.A., Camble R., Colls J., Rosenbrock G., Taylor I., Egerton M., Tucker A.D., Tunnicliffe A., Mistry A., Mancia F.et al. Crystal structure of the anti-fungal target N-myristoyl transferase. Nat. Struct. Biol. 5:1998;213-221.