1e4e
From Proteopedia
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Revision as of 08:00, 30 October 2007
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D-ALANYL-D-LACATE LIGASE
Overview
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.
About this Structure
1E4E is a [Protein complex] structure of sequences from [Enterococcus faecium] with MG, SO4, ADP, PHY and GOL as [ligands]. Structure known Active Sites: AC1, AC2, AC3 and AC4. Full crystallographic information is available from [OCA].
Reference
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
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Categories: Enterococcus faecium | Protein complex | Roper, D.I. | ADP | GOL | MG | PHY | SO4 | Antibiotic resistance | Cell wall | Ligase | Membrane | Peptidoglycan synthesis | Plasmid