3t14

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==Crystal structure of sulfide:quinone oxidoreductase Cys128Ala variant from Acidithiobacillus ferrooxidans with bound disulfide==
==Crystal structure of sulfide:quinone oxidoreductase Cys128Ala variant from Acidithiobacillus ferrooxidans with bound disulfide==
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<StructureSection load='3t14' size='340' side='right' caption='[[3t14]], [[Resolution|resolution]] 2.21&Aring;' scene=''>
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<StructureSection load='3t14' size='340' side='right'caption='[[3t14]], [[Resolution|resolution]] 2.21&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3t14]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Acif2 Acif2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T14 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3T14 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3t14]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acidithiobacillus_ferrooxidans_ATCC_23270 Acidithiobacillus ferrooxidans ATCC 23270]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T14 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T14 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=H2S:HYDROSULFURIC+ACID'>H2S</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=S2H:HYDROGEN+DISULFIDE'>S2H</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.21&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3kpg|3kpg]], [[3kpi|3kpi]], [[3kpk|3kpk]], [[3hyv|3hyv]], [[3hyw|3hyw]], [[3hyx|3hyx]], [[3sx6|3sx6]], [[3sxi|3sxi]], [[3sy4|3sy4]], [[3syi|3syi]], [[3sz0|3sz0]], [[3szc|3szc]], [[3szf|3szf]], [[3szw|3szw]], [[3t0k|3t0k]], [[3t2k|3t2k]], [[3t2y|3t2y]], [[3t2z|3t2z]], [[3t31|3t31]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=H2S:HYDROSULFURIC+ACID'>H2S</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AFE_1792 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243159 ACIF2])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3t14 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t14 OCA], [https://pdbe.org/3t14 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t14 RCSB], [https://www.ebi.ac.uk/pdbsum/3t14 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t14 ProSAT]</span></td></tr>
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<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=3t14 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t14 OCA], [http://pdbe.org/3t14 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3t14 RCSB], [http://www.ebi.ac.uk/pdbsum/3t14 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3t14 ProSAT]</span></td></tr>
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</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SQRD_ACIF2 SQRD_ACIF2] Catalyzes the oxidation of hydrogen sulfide, with the help of a quinone. Consecutive reaction cycles lead to the accumulation of a polysulfide product on the active site Cys residues; these products are released when they exceed a critical length, typically as cyclooctasulfur.<ref>PMID:20303979</ref> <ref>PMID:22542586</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 3t14" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 3t14" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Quinone reductase 3D structures|Quinone reductase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Acif2]]
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[[Category: Acidithiobacillus ferrooxidans ATCC 23270]]
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[[Category: Cherney, M M]]
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[[Category: Large Structures]]
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[[Category: James, M N.G]]
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[[Category: Cherney MM]]
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[[Category: Weiner, J H]]
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[[Category: James MNG]]
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[[Category: Zhang, Y]]
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[[Category: Weiner JH]]
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[[Category: Complex with disulfide]]
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[[Category: Zhang Y]]
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[[Category: Cys128ala variant]]
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[[Category: Integral monotopic membrane protein]]
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[[Category: Oxidoreductase]]
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[[Category: Sulfide:quinone oxidoreductase]]
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Current revision

Crystal structure of sulfide:quinone oxidoreductase Cys128Ala variant from Acidithiobacillus ferrooxidans with bound disulfide

PDB ID 3t14

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OCA

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