1r44
From Proteopedia
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- | [[Image:1r44.jpg|left|200px]] | + | [[Image:1r44.jpg|left|200px]] |
- | + | ||
- | '''Crystal Structure of VanX''' | + | {{Structure |
+ | |PDB= 1r44 |SIZE=350|CAPTION= <scene name='initialview01'>1r44</scene>, resolution 2.25Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= VANX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1352 Enterococcus faecium]) | ||
+ | }} | ||
+ | |||
+ | '''Crystal Structure of VanX''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1R44 is a [ | + | 1R44 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterococcus_faecium Enterococcus faecium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R44 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9702193 9702193] |
[[Category: Enterococcus faecium]] | [[Category: Enterococcus faecium]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: vanx]] | [[Category: vanx]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:46:34 2008'' |
Revision as of 11:46, 20 March 2008
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, resolution 2.25Å | |||||||
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Ligands: | |||||||
Gene: | VANX (Enterococcus faecium) | ||||||
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
Page seeded by OCA on Thu Mar 20 13:46:34 2008
Categories: Enterococcus faecium | Single protein | Holzman, T. | Katz, L. | Park, C H. | Pratt, S D. | Severin, J M. | ZN | Dipeptidase | E faecium | Vanx