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| - | [[Image:1w3p.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1w3p| PDB=1w3p | SCENE= }} | | {{STRUCTURE_1w3p| PDB=1w3p | SCENE= }} |
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| - | '''NIMA FROM D. RADIODURANS WITH A HIS71-PYRUVATE RESIDUE'''
| + | ===NIMA FROM D. RADIODURANS WITH A HIS71-PYRUVATE RESIDUE=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15492014}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15492014 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15492014}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Deinococcus radioduran]] | | [[Category: Deinococcus radioduran]] |
| | [[Category: Nim gene]] | | [[Category: Nim gene]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:06:57 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:01:05 2008'' |
Revision as of 02:01, 29 July 2008
Template:STRUCTURE 1w3p
NIMA FROM D. RADIODURANS WITH A HIS71-PYRUVATE RESIDUE
Template:ABSTRACT PUBMED 15492014
About this Structure
1W3P 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
Page seeded by OCA on Tue Jul 29 05:01:05 2008
