1IOV

COMPLEX OF D-ALA:D-ALA LIGASE WITH ADP AND A PHOSPHORYL PHOSPHONATE

1IOV の概要

• エントリーDOI: 10.2210/pdb1iov/pdb
• 分子名称: D-ALA\:D-ALA LIGASE, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: glycogen phosphorylase, ligase, cell wall, peptidoglycan synthesis, vancomycin, adp binding
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm: P07862
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33658.84

構造登録者

Knox, J.R.,Moews, P.C.,Fan, C. (登録日: 1996-09-20, 公開日: 1997-02-12, 最終更新日: 2024-05-22)

主引用文献

Fan, C.,Park, I.S.,Walsh, C.T.,Knox, J.R.
D-alanine:D-alanine ligase: phosphonate and phosphinate intermediates with wild type and the Y216F mutant.
Biochemistry, 36:2531-2538, 1997

PubMed Abstract: The crystallographic structure of the D-alanine:D-alanine ligase of the ddlB gene of Escherichia coli complexed with a D-Ala-D-alpha-hydroxybutyrate phosphonate and the structure of the Y216F mutant ligase complexed with a D-Ala-D-Ala phosphinate have been determined to 2.2 and 1.9 A resolution, respectively, and refined to R factors of 0.156 and 0.158. In each complex the inhibitor has reacted with ATP to produce ADP and a tight-binding phosphorylated transition state intermediate. Comparison of these two structures with the known crystal structure of the phosphinate intermediate of the wild-type ligase shows no major conformational changes, but B factors indicate differences in mobility of loops covering the binding site. The weaker inhibition of the Y216F mutant by both inhibitors is thought to be due in part to the loss of an interloop hydrogen bond. A similar mechanism may account for poor inhibition of VanA, the homologous D-Ala:D-lactate ligase produced by vancomycin-resistant enterococci.

PubMed: 9054558
DOI: 10.1021/bi962431t

実験手法

X-RAY DIFFRACTION (2.2 Å)