1r44

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1r44, resolution 2.25Å

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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 with ZN as ligand. 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

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