1R44

Crystal Structure of VanX

1R44 の概要

• エントリーDOI: 10.2210/pdb1r44/pdb
• 分子名称: D-alanyl-D-alanine dipeptidase, ZINC ION (3 entities in total)
• 機能のキーワード: vanx, e.faecium, dipeptidase, hydrolase
• 由来する生物種: Enterococcus faecium
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 140841.46

構造登録者

Pratt, S.D.,Katz, L.,Severin, J.M.,Holzman, T.,Park, C.H. (登録日: 2003-10-03, 公開日: 2004-06-15, 最終更新日: 2024-02-14)

主引用文献

Bussiere, D.E.,Pratt, S.D.,Katz, L.,Severin, J.M.,Holzman, T.,Park, C.H.
The Structure of VanX Reveals a Novel Amino-Dipeptidase Involved in Mediating Transposon-Based Vancomycin Resistance
Mol.Cell, 2:75-84, 1998

PubMed Abstract: VanX is a zinc-dependent D-alanyl-D-alanine dipeptidase that is a critical component in a system that mediates transposon-based vancomycin resistance in enterococci. It is also a key drug target in circumventing clinical vancomycin resistance. The structure of VanX from E. faecium has been solved by X-ray crystallography and reveals a Zn(2+)-dipeptidase with a unique overall fold and a well-defined active site confined within a cavity of limited size. The crystal structures of VanX, the VanX:D-alanyl-D-alanine complex, the VanX:D-alanine complex, and VanX in complex with phosphonate and phosphinate transition-state analog inhibitors, are also presented at high resolution. Structural homology searches of known structures revealed that the fold of VanX is similar to those of two proteins: the N-terminal fragment of murine Sonic hedgehog and the Zn(2+)-dependent N-acyl-D-alanyl-D-alanine carboxypeptidase of S. albus G.

PubMed: 9702193
DOI: 10.1016/S1097-2765(00)80115-X

実験手法

X-RAY DIFFRACTION (2.25 Å)