1w3o
From Proteopedia
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|PDB= 1w3o |SIZE=350|CAPTION= <scene name='initialview01'>1w3o</scene>, resolution 1.60Å | |PDB= 1w3o |SIZE=350|CAPTION= <scene name='initialview01'>1w3o</scene>, resolution 1.60Å | ||
|SITE= <scene name='pdbsite=AC1:Pyr+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Pyr+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene> | + | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1w3o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w3o OCA], [http://www.ebi.ac.uk/pdbsum/1w3o PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1w3o RCSB]</span> | ||
}} | }} | ||
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[[Category: Mcsweeney, S M.]] | [[Category: Mcsweeney, S M.]] | ||
[[Category: Terradot, L.]] | [[Category: Terradot, L.]] | ||
| - | [[Category: ACT]] | ||
| - | [[Category: PYR]] | ||
[[Category: 5-nitroimidazole resistance]] | [[Category: 5-nitroimidazole resistance]] | ||
[[Category: antibiotic resistance]] | [[Category: antibiotic resistance]] | ||
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[[Category: nim gene]] | [[Category: nim gene]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:30:44 2008'' |
Revision as of 21:30, 30 March 2008
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| , resolution 1.60Å | |||||||
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| Sites: | |||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF NIMA FROM D. RADIODURANS
Overview
5-Nitroimidazole-based antibiotics are compounds extensively used for treating infections in humans and animals caused by several important pathogens. They are administered as prodrugs, and their activation depends upon an anaerobic 1-electron reduction of the nitro group by a reduction pathway in the cells. Bacterial resistance toward these drugs is thought to be caused by decreased drug uptake and/or an altered reduction efficiency. One class of resistant strains, identified in Bacteroides, has been shown to carry Nim genes (NimA, -B, -C, -D, and -E), which encode for reductases that convert the nitro group on the antibiotic into a non-bactericidal amine. In this paper, we have described the crystal structure of NimA from Deinococcus radiodurans (drNimA) at 1.6 A resolution. We have shown that drNimA is a homodimer in which each monomer adopts a beta-barrel fold. We have identified the catalytically important His-71 along with the cofactor pyruvate and antibiotic binding sites, all of which are found at the monomer-monomer interface. We have reported three additional crystal structures of drNimA, one in which the antibiotic metronidazole is bound to the protein, one with pyruvate covalently bound to His-71, and one with lactate covalently bound to His-71. Based on these structures, a reaction mechanism has been proposed in which the 2-electron reduction of the antibiotic prevents accumulation of the toxic nitro radical. This mechanism suggests that Nim proteins form a new class of reductases, conferring resistance against 5-nitroimidazole-based antibiotics.
About this Structure
1W3O is a Single protein structure of sequence from Deinococcus radiodurans. Full crystallographic information is available from OCA.
Reference
Structural basis of 5-nitroimidazole antibiotic resistance: the crystal structure of NimA from Deinococcus radiodurans., Leiros HK, Kozielski-Stuhrmann S, Kapp U, Terradot L, Leonard GA, McSweeney SM, J Biol Chem. 2004 Dec 31;279(53):55840-9. Epub 2004 Oct 18. PMID:15492014
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