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| | ==High resolution crystal structure of the antibiotic resistance protein NimA from Deinococcus radiodurans== | | ==High resolution crystal structure of the antibiotic resistance protein NimA from Deinococcus radiodurans== |
| - | <StructureSection load='2vpa' size='340' side='right' caption='[[2vpa]], [[Resolution|resolution]] 1.20Å' scene=''> | + | <StructureSection load='2vpa' size='340' side='right'caption='[[2vpa]], [[Resolution|resolution]] 1.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2vpa]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_radiodurans"_raj_et_al._1960 "micrococcus radiodurans" raj et al. 1960]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VPA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VPA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2vpa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VPA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VPA FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1w3q|1w3q]], [[1w3o|1w3o]], [[1w3p|1w3p]], [[1w3r|1w3r]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vpa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vpa OCA], [http://pdbe.org/2vpa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vpa RCSB], [http://www.ebi.ac.uk/pdbsum/2vpa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vpa ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vpa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vpa OCA], [https://pdbe.org/2vpa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vpa RCSB], [https://www.ebi.ac.uk/pdbsum/2vpa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vpa ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9RW27_DEIRA Q9RW27_DEIRA] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Micrococcus radiodurans raj et al. 1960]] | + | [[Category: Deinococcus radiodurans]] |
| - | [[Category: Leiros, H K.S]] | + | [[Category: Large Structures]] |
| - | [[Category: McSweeney, S M]] | + | [[Category: Leiros H-KS]] |
| - | [[Category: Tedesco, C]] | + | [[Category: McSweeney SM]] |
| - | [[Category: Atomic resolution]] | + | [[Category: Tedesco C]] |
| - | [[Category: Cofactor]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
Q9RW27_DEIRA
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Many anaerobic human pathogenic bacteria are treated using 5-nitroimidazole-based (5-Ni) antibiotics, a class of inactive prodrugs that contain a nitro group. The nitro group must be activated in an anaerobic one-electron reduction and is therefore dependent on the redox system in the target cells. Antibiotic resistance towards 5-Ni drugs is found to be related to the nim genes (nimA, nimB, nimC, nimD, nimE and nimF), which are proposed to encode a reductase that is responsible for converting the nitro group of the antibiotic into a nonbactericidal amine. A mechanism for the Nim enzyme has been proposed in which two-electron reduction of the nitro group leads to the generation of nontoxic derivatives and confers resistance against these antibiotics. The cofactor was found to be important in the mechanism and was found to be covalently linked to the reactive His71. In this paper, the 1.2 A atomic resolution crystal structure of the 5-nitroimidazole antibiotic resistance protein NimA from Deinococcus radiodurans (DrNimA) is presented. A planar cofactor is clearly visible and well defined in the electron-density map adjacent to His71, the identification of the cofactor and its properties are discussed.
High-resolution structure of the antibiotic resistance protein NimA from Deinococcus radiodurans.,Leiros HK, Tedesco C, McSweeney SM Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Jun 1;64(Pt 6):442-7. doi:, 10.1107/S1744309108009901. Epub 2008 May 16. PMID:18540048[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Leiros HK, Tedesco C, McSweeney SM. High-resolution structure of the antibiotic resistance protein NimA from Deinococcus radiodurans. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Jun 1;64(Pt 6):442-7. doi:, 10.1107/S1744309108009901. Epub 2008 May 16. PMID:18540048 doi:http://dx.doi.org/10.1107/S1744309108009901
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