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.
1r44
From Proteopedia
Crystal Structure of VanX
Overview
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.
About this Structure
1R44 is a Single protein structure of sequence from Enterococcus faecium. Full crystallographic information is available from OCA.
Reference
The structure of VanX reveals a novel amino-dipeptidase involved in mediating transposon-based vancomycin resistance., Bussiere DE, Pratt SD, Katz L, Severin JM, Holzman T, Park CH, Mol Cell. 1998 Jul;2(1):75-84. PMID:9702193 Page seeded by OCA on Sat May 3 07:02:55 2008
