1E4E

D-alanyl-D-lacate ligase

1E4E の概要

• エントリーDOI: 10.2210/pdb1e4e/pdb
• 関連するPDBエントリー: 1IOV 1IOW
• 分子名称: VANCOMYCIN/TEICOPLANIN A-TYPE RESISTANCE PROTEIN VANA, ADENOSINE-5'-DIPHOSPHATE, 1(S)-AMINOETHYL-(2-CARBOXYPROPYL)PHOSPHORYL-PHOSPHINIC ACID, ... (8 entities in total)
• 機能のキーワード: ligase, cell wall, antibiotic resistance, membrane, peptidoglycan synthesis
• 由来する生物種: ENTEROCOCCUS FAECIUM; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 78272.58

構造登録者

Roper, D.I. (登録日: 2000-07-03, 公開日: 2001-06-28, 最終更新日: 2024-10-09)

主引用文献

Roper, D.I.,Huyton, T.,Vagin, A.,Dodson, G.
The molecular basis of vancomycin resistance in clinically relevant Enterococci: crystal structure of D-alanyl-D-lactate ligase (VanA).
Proc. Natl. Acad. Sci. U.S.A., 97:8921-8925, 2000

PubMed Abstract: 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.

PubMed: 10908650
DOI: 10.1073/pnas.150116497

実験手法

X-RAY DIFFRACTION (2.5 Å)