View source for 3ttb


==Structure of the Thioalkalivibrio paradoxus cytochrome c nitrite reductase in complex with sulfite==
<StructureSection load='3ttb' size='340' side='right'caption='[[3ttb]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3ttb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thioalkalivibrio_paradoxus Thioalkalivibrio paradoxus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TTB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TTB 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]] 2&#8491;</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=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=SO3:SULFITE+ION'>SO3</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3ttb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ttb OCA], [https://pdbe.org/3ttb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ttb RCSB], [https://www.ebi.ac.uk/pdbsum/3ttb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ttb ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/E7EDQ7_9GAMM E7EDQ7_9GAMM] Plays a role in nitrite reduction.[SAAS:SAAS00096633]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Octaheme nitrite reductase from the haloalkaliphilic bacterium Thioalkalivibrio paradoxus was isolated and characterized. A comparative structural and functional analysis of two homologous octaheme nitrite reductases from closely related Thioalkalivibrio species was performed. It was shown that both enzymes have similar catalytic properties due to high structural similarity. Both enzymes are characterized by specific structural features distinguishing them from pentaheme cytochrome c nitrite reductases, such as the Tyr-Cys bond in the active site, the hexameric structure resulting in the formation of a void space inside the hexamer, and the product channel that opens into the void interior space of the hexamer. It is suggested that these specific structural features are responsible for the higher nitrite reductase activity, the greater preference for nitrite than sulfite as a substrate, and the wider pH range of the catalytic activity of octaheme nitrite reductases compared to pentaheme homologues. (c) 2012 The Authors Journal compilation (c) 2012 FEBS.

Comparative structural and functional analysis of two octaheme nitrite reductases from closely related Thioalkalivibrio species.,Tikhonova T, Tikhonov A, Trofimov A, Polyakov K, Boyko K, Cherkashin E, Rakitina T, Sorokin D, Popov V FEBS J. 2012 Aug 30. doi: 10.1111/j.1742-4658.2012.08811.x. PMID:22935005<ref>PMID:22935005</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3ttb" style="background-color:#fffaf0;"></div>

==See Also==
*[[Cytochrome c nitrite reductase|Cytochrome c nitrite reductase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thioalkalivibrio paradoxus]]
[[Category: Dorovatovskii PV]]
[[Category: Polyakov KM]]
[[Category: Popov VO]]
[[Category: Tikhonov AV]]
[[Category: Tikhonova TV]]
[[Category: Trofimov AA]]