Crystallization and preliminary X-ray analysis of a D-Ala:D-Ser ligase associated with VanG-type vancomycin resistance.
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.
Institut Pasteur, Plateforme 6, CNRS URA 2185, 25 rue du Dr Roux, 75724 Paris Cedex 15, France.
Patrick
P
Weber
Djalal
D
Meziane-Cherif
Ahmed
A
Haouz
Frederick A
FA
Saul
Patrice
P
Courvalin
D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D013293:Enterococcus faecalis / Q000201:enzymology*; D010453:Peptide Synthases / Q000737:chemistry* / Q000302:isolation & purification; D020713:Vancomycin Resistance
D001426:Bacterial Proteins; D010453:Peptide Synthases; C108395:VanC protein, Enterococcus