1e4e | pdb_00001e4e

D-ALANYL-D-LACATE LIGASE

spinqualitylabelsall models 1e4e, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1e4e is a 2 chain structure with sequence from Enterococcus faecium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ADP, GOL, MG, PHY, SO4 Related: 1iow, 1iov Gene: VANA (Enterococcus faecium) Activity: D-alanine--(R)-lactate ligase, with EC number 6.1.2.1 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed d-alanine-d-lactate ligase from Enterococcus faecium BM4147 is directly responsible for the biosynthesis of alternate cell-wall precursors in bacteria, which are resistant to the glycopeptide antibiotic vancomycin. The crystal structure has been determined with data extending to 2.5-A resolution. This structure shows that the active site has unexpected interactions and is distinct from previous models for d-alanyl-d-lactate ligase mechanistic studies. It appears that the preference of the enzyme for lactate as a ligand over d-alanine could be mediated by electrostatic effects and/or a hydrogen-bonding network, which principally involve His-244. The structure of d-alanyl-d-lactate ligase provides a revised interpretation of the molecular events that lead to vancomycin resistance. The molecular basis of vancomycin resistance in clinically relevant Enterococci: crystal structure of D-alanyl-D-lactate ligase (VanA).,Roper DI, Huyton T, Vagin A, Dodson G Proc Natl Acad Sci U S A. 2000 Aug 1;97(16):8921-5. PMID:10908650 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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