1r44
From Proteopedia
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|PDB= 1r44 |SIZE=350|CAPTION= <scene name='initialview01'>1r44</scene>, resolution 2.25Å | |PDB= 1r44 |SIZE=350|CAPTION= <scene name='initialview01'>1r44</scene>, resolution 2.25Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= VANX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1352 Enterococcus faecium]) | |GENE= VANX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1352 Enterococcus faecium]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1r44 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r44 OCA], [http://www.ebi.ac.uk/pdbsum/1r44 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1r44 RCSB]</span> | ||
}} | }} | ||
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[[Category: Pratt, S D.]] | [[Category: Pratt, S D.]] | ||
[[Category: Severin, J M.]] | [[Category: Severin, J M.]] | ||
| - | [[Category: ZN]] | ||
[[Category: dipeptidase]] | [[Category: dipeptidase]] | ||
[[Category: e faecium]] | [[Category: e faecium]] | ||
[[Category: vanx]] | [[Category: vanx]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:22:59 2008'' |
Revision as of 20:23, 30 March 2008
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| , resolution 2.25Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | VANX (Enterococcus faecium) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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