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© Ahmed Haouz
Cristaux d'une protéine de Mycobacterium tuberculosis produits dans le cadre du Grand Programme Horizontal sur la Tuberculose à l'Institut Pasteur. La caractérisation structurale de protéines mycobactériennes aide à une meilleure compréhension de la physiologie et de la pathogénicité des mycobactéries et fournit un point de départ pour la conception de nouveaux agents antibactériens.
Publication : Acta crystallographica. Section F, Structural biology and crystallization communications

Crystallization and preliminary X-ray analysis of a D-Ala:D-Ser ligase associated with VanG-type vancomycin resistance

Team: Crystallography
Member: Ahmed Haouz
Member: Frederick Saul
Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Acta crystallographica. Section F, Structural biology and crystallization communications - 23 Sep 2009

Weber P, Meziane-Cherif D, Haouz A, Saul FA, Courvalin P

Link to Pubmed [PMID] – 19851013

Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 2009 Oct;65(Pt 10):1024-6

Acquired VanG-type resistance to vancomycin in Enterococcus faecalis BM4518 arises from inducible synthesis of peptidoglycan precursors ending in D-alanyl-D-serine, to which vancomycin exhibits low binding affinity. VanG, a D-alanine:D-serine ligase, catalyzes the ATP-dependent synthesis of the D-Ala-D-Ser dipeptide, which is incorporated into the peptidoglycan synthesis of VanG-type vancomycin-resistant strains. Here, the purification, crystallization and preliminary crystallographic analysis of VanG in complex with ADP are reported. The crystal belonged to space group P3(1)21, with unit-cell parameters a = b = 116.1, c = 177.2 A, and contained two molecules in the asymmetric unit. A complete data set has been collected to 2.35 A resolution from a single crystal under cryogenic conditions using synchrotron radiation.