3uu9: Difference between revisions

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'''Unreleased structure'''


The entry 3uu9 is ON HOLD  until Paper Publication
==Structure of the free TvNiRb form of Thioalkalivibrio nitratireducens cytochrome c nitrite reductase==
<StructureSection load='3uu9' size='340' side='right'caption='[[3uu9]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3uu9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thioalkalivibrio_nitratireducens Thioalkalivibrio nitratireducens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UU9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UU9 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]] 2.2&#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=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</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=3uu9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uu9 OCA], [https://pdbe.org/3uu9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uu9 RCSB], [https://www.ebi.ac.uk/pdbsum/3uu9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uu9 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NIR_THIND NIR_THIND] Catalyzes the reduction of nitrite to ammonia, consuming six electrons in the process (PubMed:16500161, PubMed:22281743). Has very low activity toward hydroxylamine (PubMed:16500161). Has even lower activity toward sulfite (PubMed:16500161, PubMed:22281743). Sulfite reductase activity is maximal at neutral pH (PubMed:20944237).<ref>PMID:16500161</ref> <ref>PMID:20944237</ref> <ref>PMID:22281743</ref>


Authors: Trofimov, A.A., Polyakov, K.M., Tikhonova, T.V., Tikhonov, A.V., Dorovatovskii, P.V., Popov, V.O.
==See Also==
 
*[[Cytochrome c nitrite reductase|Cytochrome c nitrite reductase]]
Description: Structure of the free TvNiRb form of Thioalkalivibrio nitratireducens cytochrome c nitrite reductase
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thioalkalivibrio nitratireducens]]
[[Category: Dorovatovskii PV]]
[[Category: Polyakov KM]]
[[Category: Popov VO]]
[[Category: Tikhonov AV]]
[[Category: Tikhonova TV]]
[[Category: Trofimov AA]]

Latest revision as of 17:08, 14 March 2024

Structure of the free TvNiRb form of Thioalkalivibrio nitratireducens cytochrome c nitrite reductaseStructure of the free TvNiRb form of Thioalkalivibrio nitratireducens cytochrome c nitrite reductase

Structural highlights

3uu9 is a 2 chain structure with sequence from Thioalkalivibrio nitratireducens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NIR_THIND Catalyzes the reduction of nitrite to ammonia, consuming six electrons in the process (PubMed:16500161, PubMed:22281743). Has very low activity toward hydroxylamine (PubMed:16500161). Has even lower activity toward sulfite (PubMed:16500161, PubMed:22281743). Sulfite reductase activity is maximal at neutral pH (PubMed:20944237).[1] [2] [3]

See Also

References

  1. ↑ Tikhonova TV, Slutsky A, Antipov AN, Boyko KM, Polyakov KM, Sorokin DY, Zvyagilskaya RA, Popov VO. Molecular and catalytic properties of a novel cytochrome c nitrite reductase from nitrate-reducing haloalkaliphilic sulfur-oxidizing bacterium Thioalkalivibrio nitratireducens. Biochim Biophys Acta. 2006 Apr;1764(4):715-23. Epub 2006 Feb 9. PMID:16500161 doi:http://dx.doi.org/10.1016/j.bbapap.2005.12.021
  2. ↑ Trofimov AA, Polyakov KM, Boyko KM, Tikhonova TV, Safonova TN, Tikhonov AV, Popov AN, Popov VO. Structures of complexes of octahaem cytochrome c nitrite reductase from Thioalkalivibrio nitratireducens with sulfite and cyanide. Acta Crystallogr D Biol Crystallogr. 2010 Oct;66(Pt 10):1043-7. Epub 2010, Sep 18. PMID:20944237 doi:10.1107/S0907444910031665
  3. ↑ Trofimov AA, Polyakov KM, Tikhonova TV, Tikhonov AV, Safonova TN, Boyko KM, Dorovatovskii PV, Popov VO. Covalent modifications of the catalytic tyrosine in octahaem cytochrome c nitrite reductase and their effect on the enzyme activity. Acta Crystallogr D Biol Crystallogr. 2012 Feb;68(Pt 2):144-53. Epub 2012, Jan 13. PMID:22281743 doi:10.1107/S0907444911052632

3uu9, resolution 2.20Å

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