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

Abstract : Acquired VanG-type resistance to vancomycin in Enterococcus faecalis BM4518 arises from inducible synthesis of peptidoglycan precursors ending in d-alanyld-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 Å , and contained two molecules in the asymmetric unit. A complete data set has been collected to 2.35 Å resolution from a single crystal under cryogenic conditions using synchrotron radiation.
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Patrick Weber, Djalal Meziane-Cherif, Ahmed Haouz, Frederick A. Saul, Patrice Courvalin. Crystallization and preliminary X-ray analysis of aD-Ala:D-Ser ligase associated with VanG-type vancomycin resistance. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, International Union of Crystallography, 2009, 65 (10), pp.1024 - 1026. ⟨10.1107/s1744309109033831⟩. ⟨pasteur-03525336⟩

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