1r44
From Proteopedia
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'''Crystal Structure of VanX''' | '''Crystal Structure of VanX''' | ||
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[[Category: Pratt, S D.]] | [[Category: Pratt, S D.]] | ||
[[Category: Severin, J M.]] | [[Category: Severin, J M.]] | ||
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| - | [[Category: | + | [[Category: E faecium]] |
| - | [[Category: | + | [[Category: Vanx]] |
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Revision as of 04:02, 3 May 2008
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
