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New page: left|200px<br /><applet load="1fs7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fs7, resolution 1.60Å" /> '''CYTOCHROME C NITRITE... |
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== | ==CYTOCHROME C NITRITE REDUCTASE FROM WOLINELLA SUCCINOGENES== | ||
Cytochrome c nitrite reductase catalyzes the 6-electron reduction of | <StructureSection load='1fs7' size='340' side='right'caption='[[1fs7]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1fs7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Wolinella_succinogenes Wolinella succinogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FS7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FS7 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=Y1:YTTRIUM+ION'>Y1</scene></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=1fs7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fs7 OCA], [https://pdbe.org/1fs7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fs7 RCSB], [https://www.ebi.ac.uk/pdbsum/1fs7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fs7 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/NRFA_WOLSU NRFA_WOLSU] Plays a role in nitrite reduction.<ref>PMID:10672190</ref> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fs/1fs7_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fs7 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Cytochrome c nitrite reductase catalyzes the 6-electron reduction of nitrite to ammonia. This second part of the respiratory pathway of nitrate ammonification is a key step in the biological nitrogen cycle. The x-ray structure of the enzyme from the epsilon-proteobacterium Wolinella succinogenes has been solved to a resolution of 1.6 A. It is a pentaheme c-type cytochrome whose heme groups are packed in characteristic motifs that also occur in other multiheme cytochromes. Structures of W. succinogenes nitrite reductase have been obtained with water bound to the active site heme iron as well as complexes with two inhibitors, sulfate and azide, whose binding modes and inhibitory functions differ significantly. Cytochrome c nitrite reductase is part of a highly optimized respiratory system found in a wide range of Gram-negative bacteria. It reduces both anionic and neutral substrates at the distal side of a lysine-coordinated high-spin heme group, which is accessible through two different channels, allowing for a guided flow of reaction educt and product. Based on sequence comparison and secondary structure prediction, we have demonstrated that cytochrome c nitrite reductases constitute a protein family of high structural similarity. | |||
Cytochrome c nitrite reductase from Wolinella succinogenes. Structure at 1.6 A resolution, inhibitor binding, and heme-packing motifs.,Einsle O, Stach P, Messerschmidt A, Simon J, Kroger A, Huber R, Kroneck PM J Biol Chem. 2000 Dec 15;275(50):39608-16. PMID:10984487<ref>PMID:10984487</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
Cytochrome c nitrite reductase | </div> | ||
[[Category: | <div class="pdbe-citations 1fs7" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]] | |||
*[[Cytochrome c nitrite reductase|Cytochrome c nitrite reductase]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Wolinella succinogenes]] | [[Category: Wolinella succinogenes]] | ||
[[Category: Einsle | [[Category: Einsle O]] | ||
[[Category: Huber | [[Category: Huber R]] | ||
[[Category: Kroeger | [[Category: Kroeger A]] | ||
[[Category: Kroneck | [[Category: Kroneck PMH]] | ||
[[Category: Messerschmidt | [[Category: Messerschmidt A]] | ||
[[Category: Simon | [[Category: Simon J]] | ||
[[Category: Stach | [[Category: Stach P]] | ||
Latest revision as of 11:26, 6 November 2024
CYTOCHROME C NITRITE REDUCTASE FROM WOLINELLA SUCCINOGENESCYTOCHROME C NITRITE REDUCTASE FROM WOLINELLA SUCCINOGENES
Structural highlights
FunctionNRFA_WOLSU Plays a role in nitrite reduction.[1] 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 PubMedCytochrome c nitrite reductase catalyzes the 6-electron reduction of nitrite to ammonia. This second part of the respiratory pathway of nitrate ammonification is a key step in the biological nitrogen cycle. The x-ray structure of the enzyme from the epsilon-proteobacterium Wolinella succinogenes has been solved to a resolution of 1.6 A. It is a pentaheme c-type cytochrome whose heme groups are packed in characteristic motifs that also occur in other multiheme cytochromes. Structures of W. succinogenes nitrite reductase have been obtained with water bound to the active site heme iron as well as complexes with two inhibitors, sulfate and azide, whose binding modes and inhibitory functions differ significantly. Cytochrome c nitrite reductase is part of a highly optimized respiratory system found in a wide range of Gram-negative bacteria. It reduces both anionic and neutral substrates at the distal side of a lysine-coordinated high-spin heme group, which is accessible through two different channels, allowing for a guided flow of reaction educt and product. Based on sequence comparison and secondary structure prediction, we have demonstrated that cytochrome c nitrite reductases constitute a protein family of high structural similarity. Cytochrome c nitrite reductase from Wolinella succinogenes. Structure at 1.6 A resolution, inhibitor binding, and heme-packing motifs.,Einsle O, Stach P, Messerschmidt A, Simon J, Kroger A, Huber R, Kroneck PM J Biol Chem. 2000 Dec 15;275(50):39608-16. PMID:10984487[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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