1e4e | pdb_00001e4e
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| 1e4e, resolution 2.5Å | |||||||||||||
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| Sites: | AC1, AC2, AC3 and AC4 | ||||||||||||
| Ligands: | MG, SO4, ADP, PHY and GOL | ||||||||||||
| Gene: | VANA (Enterococcus faecium) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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. 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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