Structural highlights
Function
[VANX_ENTFC] Catalyzes hydrolysis of the D-alanyl-D-alanine dipeptide.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bussiere DE, Pratt SD, Katz L, Severin JM, Holzman T, Park CH. The structure of VanX reveals a novel amino-dipeptidase involved in mediating transposon-based vancomycin resistance. Mol Cell. 1998 Jul;2(1):75-84. PMID:9702193
