Crystallization and preliminary X-ray characterization of VanA from Enterococcus faecium BM4147: towards the molecular basis of bacterial resistance to the glycopeptide antibiotic vancomycin.
A recombinant form of Enterococcus facieum BM4147 D-alanine-D-lactate ligase (VanA) has been prepared and crystallized. VanA was found to crystallize only in the presence of a phosphinate inhibitor analogue of D-alanine-D-alanine. The crystals grow in 40-45% ammonium sulfate, 0.1 M 3-(N-morpholino)-propanesulfonic acid pH 6.0 and reach dimensions of 0.4 x 0.2 x 0.1 mm. The crystals diffract to at least 2.5 A and are in the centred orthorhombic space group C222(1), with unit-cell dimensions a = 123.2, b = 225.4, c = 72.4 A.
Huyton
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Structural Biology Laboratory, Department of Chemistry, The University of York, Heslington, York YO10 5DD, England.
Roper
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D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification*; D019729:Carbon-Oxygen Ligases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification*; D003460:Crystallization; D018360:Crystallography, X-Ray; D004352:Drug Resistance, Microbial; D016984:Enterococcus faecium / Q000201:enzymology* / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D013379:Substrate Specificity; D014640:Vancomycin / Q000494:pharmacology
D001426:Bacterial Proteins; D011994:Recombinant Proteins; C071437:VanA ligase, Bacteria; D014640:Vancomycin; D019729:Carbon-Oxygen Ligases