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| | <StructureSection load='3l1t' size='340' side='right'caption='[[3l1t]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='3l1t' size='340' side='right'caption='[[3l1t]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3l1t]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L1T OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3L1T FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3l1t]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L1T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3L1T FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=SO3:SULFITE+ION'>SO3</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]] 2.3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2rdz|2rdz]], [[3bnf|3bnf]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=SO3:SULFITE+ION'>SO3</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nitrite_reductase_(cytochrome;_ammonia-forming) Nitrite reductase (cytochrome; ammonia-forming)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.2.2 1.7.2.2] </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=3l1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l1t OCA], [https://pdbe.org/3l1t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3l1t RCSB], [https://www.ebi.ac.uk/pdbsum/3l1t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3l1t ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3l1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l1t OCA], [http://pdbe.org/3l1t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3l1t RCSB], [http://www.ebi.ac.uk/pdbsum/3l1t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3l1t ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/NRFA_ECOLI NRFA_ECOLI]] Plays a role in nitrite reduction.[HAMAP-Rule:MF_01182] | + | [https://www.uniprot.org/uniprot/NRFA_ECOLI NRFA_ECOLI] Plays a role in nitrite reduction.[HAMAP-Rule:MF_01182] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| | *[[Cytochrome c nitrite reductase|Cytochrome c nitrite reductase]] | | *[[Cytochrome c nitrite reductase|Cytochrome c nitrite reductase]] |
| - | *[[Nitrite reductase 3D structures|Nitrite reductase 3D structures]] | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Escherichia coli]] | + | [[Category: Escherichia coli K-12]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Butt, J N]] | + | [[Category: Butt JN]] |
| - | [[Category: Clarke, T A]] | + | [[Category: Clarke TA]] |
| - | [[Category: Hemmings, A M]] | + | [[Category: Hemmings AM]] |
| - | [[Category: C-type cytochrome]]
| + | |
| - | [[Category: Electron transport]]
| + | |
| - | [[Category: Heme]]
| + | |
| - | [[Category: Iron]]
| + | |
| - | [[Category: Metal-binding]]
| + | |
| - | [[Category: Multiheme]]
| + | |
| - | [[Category: Nitrite reductase]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Sulfite]]
| + | |
| - | [[Category: Transport]]
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| Structural highlights
Function
NRFA_ECOLI Plays a role in nitrite reduction.[HAMAP-Rule:MF_01182]
Publication Abstract from PubMed
NrfA is a pentahaem cytochrome present in a wide-range of gamma-, delta- and epsilon-proteobacteria. Its nitrite and nitric oxide reductase activities have been studied extensively and contribute to respiratory nitrite ammonification and nitric oxide detoxification respectively. Sulfite is a third substrate for NrfA that may be encountered in the micro-oxic environments where nrfA is expressed. Consequently, we have performed quantitative kinetic and thermodynamic studies of the interactions between sulfite and Escherichia coli NrfA to provide a biochemical framework from which to consider their possible cellular consequences. A combination of voltammetric, spectroscopic and crystallographic analyses define dissociation constants for sulfite binding to NrfA in oxidized (~54 muM), semi-reduced (~145 muM) and reduced (~180 muM) states that are comparable with each other, and the Km (~70 muM) for sulfite reduction at pH 7. Under comparable conditions Km values of ~22 and ~300 muM describe nitrite and nitric oxide reduction respectively, whereas the affinities of nitrate and thiocyanate for NrfA fall more than 50-fold on enzyme reduction. These results are discussed in terms of the nature of sulfite co-ordination within the active site of NrfA and their implications for the cellular activity of NrfA.
Kinetic and thermodynamic resolution of the interactions between sulfite and the pentahaem cytochrome NrfA from Escherichia coli.,Kemp GL, Clarke TA, Marritt SJ, Lockwood C, Poock SR, Hemmings AM, Richardson DJ, Cheesman MR, Butt JN Biochem J. 2010 Oct 1;431(1):73-80. PMID:20629638[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kemp GL, Clarke TA, Marritt SJ, Lockwood C, Poock SR, Hemmings AM, Richardson DJ, Cheesman MR, Butt JN. Kinetic and thermodynamic resolution of the interactions between sulfite and the pentahaem cytochrome NrfA from Escherichia coli. Biochem J. 2010 Oct 1;431(1):73-80. PMID:20629638 doi:10.1042/BJ20100866
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