Structure of enterococcus faecium l, d-transpeptidase acylated by ertapenem provides insight into the inactivation mechanism

ACS Chemical Biology

Volumn 8, Issue 6, 2013, Pages 1140-1146

  Lecoq, Lauriane ^a,b,c   Dubée, Vincent ^d,e,f   Triboulet, Sébastien ^d,e,f   Bougault, Catherine ^a,b,c   Hugonnet, Jean Emmanuel ^d,e,f   Arthur, Michel ^d,e,f   Simorre, Jean Pierre ^a,b,c  

^a CEA GRENOBLE   (France)

^b INSTITUT DE BIOLOGIE STRUCTURALE   (France)

^c UNIV GRENOBLE ALPES   (France)

^d CENTRE DE RECHERCHE DES CORDELIERS   (France)

^e INSERM   (France)

^f UNIVERSITÉ PARIS DESCARTES   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ERTAPENEM; GAMMA GLUTAMYLTRANSFERASE; ANTIINFECTIVE AGENT; BETA LACTAM; PEPTIDYLTRANSFERASE;

ACYLATION; ARTICLE; BACTERIAL CELL; CARBON NUCLEAR MAGNETIC RESONANCE; CLINICAL PROTOCOL; CLOSTRIDIUM DIFFICILE; CROSS LINKING; ENTEROCOCCUS FAECIUM; ENZYME INACTIVATION; MYCOBACTERIUM ABSCESSUS; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTON NUCLEAR MAGNETIC RESONANCE; PROTON TRANSPORT; ACETYLATION; CHEMICAL STRUCTURE; CHEMISTRY; DRUG ANTAGONISM; DRUG EFFECT; ENZYMOLOGY; GRAM POSITIVE INFECTION; HUMAN; METABOLISM; MICROBIOLOGY; PROTEIN CONFORMATION;

BACTERIA (MICROORGANISMS); ENTEROCOCCUS FAECIUM; MYCOBACTERIUM TUBERCULOSIS;

ACETYLATION; ANTI-BACTERIAL AGENTS; BETA-LACTAMS; ENTEROCOCCUS FAECIUM; GRAM-POSITIVE BACTERIAL INFECTIONS; HUMANS; MODELS, MOLECULAR; PEPTIDYL TRANSFERASES; PROTEIN CONFORMATION;

EID: 84879750898     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb4001603     Document Type: Article

References (24)

1. Zapun, A., Contreras-Martel, C., and Vernet, T. (2008) Penicillin-binding proteins and β-lactam resistance FEMS Microbiol. Rev. 32, 361-385
2. Mainardi, J.-L., Fourgeaud, M., Hugonnet, J.-E., Dubost, L., Brouard, J.-P., Ouazzani, J., Rice, L. B., Gutmann, L., and Arthur, M. (2005) A novel peptidoglycan cross-linking enzyme for a β-lactam-resistant transpeptidation pathway J. Biol. Chem. 280, 38146-38152
3. Lavollay, M., Arthur, M., Fourgeaud, M., Dubost, L., Marie, A., Veziris, N., Blanot, D., Gutmann, L., and Mainardi, J.-L. (2008) The peptidoglycan of stationary-phase Mycobacterium tuberculosis predominantly contains cross-links generated by l, d -transpeptidation J. Bacteriol. 190, 4360-4366
4. Lavollay, M., Fourgeaud, M., Herrmann, J. L., Dubost, L., Marie, A., Gutmann, L., Arthur, M., and Mainardi, J.-L. (2011) The peptidoglycan of Mycobacterium abscessus is predominantly cross-linked by l, d -transpeptidases J. Bacteriol. 193, 778-782
5. Peltier, J., Courtin, P., El Meouche, I., Lemee, L., Chapot-Chartier, M. P., and Pons, J. L. (2011) Clostridium difficile has an original peptidoglycan structure with a high level of N -acetylglucosamine deacetylation and mainly 3-3 cross-links J. Biol. Chem. 286, 29053-29062
6. Sacco, E., Hugonnet, J.-E., Josseaume, N., Cremniter, J., Dubost, L., Marie, A., Patin, D., Blanot, D., Rice, L. B., Mainardi, J.-L., and Arthur, M. (2010) Activation of the l, d -transpeptidation peptidoglycan cross-linking pathway by a metallo- d, d -carboxypeptidase in Enterococcus faecium Mol. Microbiol. 75, 874-885
7. Dubée, V., Arthur, M., Fief, H., Triboulet, S., Mainardi, J.-L., Gutmann, L., Sollogoub, M., Rice, L. B., Etheve-Quelquejeu, M., and Hugonnet, J. E. (2012) Kinetic analysis of Enterococcus faecium l, d -transpeptidase inactivation by carbapenems Antimicrob. Agents Chemother. 56, 3409-3412
8. Mt1 by carbapenems and cephalosporins Antimicrob. Agents Chemother. 56, 4189-4195
9. Mainardi, J.-L., Hugonnet, J.-E., Rusconi, F., Fourgeaud, M., Dubost, L., Moumi, A. N., Delfosse, V., Mayer, C., Gutmann, L., Rice, L. B., and Arthur, M. (2007) Unexpected inhibition of peptidoglycan l, d -transpeptidase from Enterococcus faecium by the β-lactam imipenem J. Biol. Chem. 282, 30414-30422
10. Papp-Wallace, K. M., Endimiani, A., Taracila, M. A., and Bonomo, R. A. (2011) Carbapenems: past, present, and future Antimicrob. Agents Chemother. 55, 4943-4960
11. Biarrotte-Sorin, S., Hugonnet, J.-E., Delfosse, V., Mainardi, J.-L., Gutmann, L., Arthur, M., and Mayer, C. (2006) Crystal structure of a novel β-lactam-insensitive peptidoglycan transpeptidase J. Mol. Biol. 359, 533-538
12. Bielnicki, J., Devedjiev, Y., Derewenda, U., Dauter, Z., Joachimiak, A., and Derewenda, Z. S. (2005) B. subtilis YkuD protein at 2.0 Å resolution: insights into the structure and function of a novel, ubiquitous family of bacterial enzymes Proteins 62, 144-151
13. Erdemli, S. B., Gupta, R., Bishai, W. R., Lamichhane, G., Amzel, L. M., and Bianchet, M. A. (2012) Targeting the cell wall of Mycobacterium tuberculosis: structure and mechanism of l, d -transpeptidase 2 Structure 20, 1-13
14. Lecoq, L., Bougault, C., Hugonnet, J.-E., Veckerlé, C., Pessey, O., Arthur, M., and Simorre, J.-P. (2012) Dynamics induced by β-lactam antibiotics in the active site of Bacillus subtilis l, d -transpeptidase Structure 20, 850-861
15. Tipper, D. and Strominger, J. (1965) Mechanism of action of penicillins: a proposal based on their structural similarity to acyl- d -alanyl- d -alanine Proc. Natl. Acad. Sci. U.S.A. 54, 1133-1141
16. Schüttelkopf, A. W. and van Aalten, D. M. F. (2004) PRODRG: a tool for high-throughput crystallography of protein-ligand complexes Acta Crystallogr., Sect. D: Biol. Crystallogr. 60, 1355-1363
17. Brunger, A. T. (2007) Version 1.2 of the crystallography and NMR system Nat. Protoc. 2, 2728-2733
18. Triboulet, S., Arthur, M., Mainardi, J.-L., Veckerlé, C., Dubée, V., Nguekam-Moumi, A., Gutmann, L., Rice, L. B., and Hugonnet, J.-E. (2011) Inactivation kinetics of a new target of β-lactam antibiotics J. Biol. Chem. 286, 22777-22784
19. 1H nuclear magnetic resonance studies of receptor-bound cyclosporin J. Am. Chem. Soc. 112, 9015-9016
20. Shen, Y., Delaglio, F., Cornilescu, G., and Bax, A. (2009) TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shift J. Biomol. NMR 44, 213-223
21. Guerry, P. and Herrmann, T. (2011) Comprehensive automation for NMR structure determination of proteins, in Methods in Molecular Biology, pp 429-451, Humana Press, New York.
22. Rieping, W., Habeck, M., Bardiaux, B., Bernard, A., Malliavin, T. E., and Nilges, M. (2007) ARIA2: automated NOE assignment and data integration in NMR structure calculation Bioinformatics 23, 381-382
23. Doreleijers, J. F., Sousa da Silva, A. W., Krieger, E., Nabuurs, S. B., Spronk, C. A. E. M., Stevens, T. J., Vranken, W. F., Vriend, G., and Vuister, G. W. (2012) CING: an integrated residue-based structure validation program suite J. Biomol. NMR 54, 267-283
24. Wallace, A., Laskowski, R., and Thornton, J. (1995) LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions Protein Eng. 8, 127-134