This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1e4e
From Proteopedia
|
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 , , , and as ligands. Known structural/functional Sites: , , and . 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
Page seeded by OCA on Thu Feb 21 12:23:44 2008
Categories: Enterococcus faecium | Protein complex | Roper, D I. | ADP | GOL | MG | PHY | SO4 | Antibiotic resistance | Cell wall | Ligase | Membrane | Peptidoglycan synthesis | Plasmid
