3szc: Difference between revisions

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==Crystal structure of sulfide:quinone oxidoreductase from Acidithiobacillus ferrooxidans in complex with gold (I) cyanide==
==Crystal structure of sulfide:quinone oxidoreductase from Acidithiobacillus ferrooxidans in complex with gold (I) cyanide==
<StructureSection load='3szc' size='340' side='right' caption='[[3szc]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='3szc' size='340' side='right'caption='[[3szc]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3szc]] 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=3SZC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SZC FirstGlance]. <br>
<table><tr><td colspan='2'>[[3szc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acif2 Acif2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SZC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SZC FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AU:GOLD+ION'>AU</scene>, <scene name='pdbligand=DCQ:2-DECYL-5,6-DIMETHOXY-3-METHYLCYCLOHEXA-2,5-DIENE-1,4-DIONE'>DCQ</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=H2S:HYDROSULFURIC+ACID'>H2S</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AU:GOLD+ION'>AU</scene>, <scene name='pdbligand=DCQ:2-DECYL-5,6-DIMETHOXY-3-METHYLCYCLOHEXA-2,5-DIENE-1,4-DIONE'>DCQ</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=H2S:HYDROSULFURIC+ACID'>H2S</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<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]], [[3szf|3szf]], [[3szw|3szw]], [[3t0k|3t0k]], [[3t14|3t14]], [[3t2k|3t2k]], [[3t2y|3t2y]], [[3t2z|3t2z]], [[3t31|3t31]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3kpg|3kpg]], [[3kpi|3kpi]], [[3kpk|3kpk]], [[3hyv|3hyv]], [[3hyw|3hyw]], [[3hyx|3hyx]], [[3sx6|3sx6]], [[3sxi|3sxi]], [[3sy4|3sy4]], [[3syi|3syi]], [[3sz0|3sz0]], [[3szf|3szf]], [[3szw|3szw]], [[3t0k|3t0k]], [[3t14|3t14]], [[3t2k|3t2k]], [[3t2y|3t2y]], [[3t2z|3t2z]], [[3t31|3t31]]</div></td></tr>
<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>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AFE_1792 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243159 ACIF2])</td></tr>
<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=3szc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3szc OCA], [http://pdbe.org/3szc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3szc RCSB], [http://www.ebi.ac.uk/pdbsum/3szc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3szc ProSAT]</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=3szc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3szc OCA], [https://pdbe.org/3szc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3szc RCSB], [https://www.ebi.ac.uk/pdbsum/3szc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3szc ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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</StructureSection>
</StructureSection>
[[Category: Acif2]]
[[Category: Acif2]]
[[Category: Large Structures]]
[[Category: Cherney, M M]]
[[Category: Cherney, M M]]
[[Category: James, M N.G]]
[[Category: James, M N.G]]

Latest revision as of 11:17, 29 June 2022

Crystal structure of sulfide:quinone oxidoreductase from Acidithiobacillus ferrooxidans in complex with gold (I) cyanideCrystal structure of sulfide:quinone oxidoreductase from Acidithiobacillus ferrooxidans in complex with gold (I) cyanide

Structural highlights

3szc is a 1 chain structure with sequence from Acif2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , , ,
Gene:AFE_1792 (ACIF2)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

Sulfide:quinone oxidoreductase (SQR) is a peripheral membrane protein that catalyzes the oxidation of sulfide species to elemental sulfur. The enzymatic reaction proceeds in two steps. The electrons from sulfides are transferred first to the enzyme cofactor, FAD, which, in turn, passes them onto the quinone pool in the membrane. Several wild-type SQR structures have been reported recently. However, the enzymatic mechanism of SQR has not been fully delineated. In order to understand the role of the catalytically essential residues in the enzymatic mechanism of SQR we produced a number of variants of the conserved residues in the catalytic site including the cysteine triad of SQR from the acidophilic, chemolithotrophic bacterium Acidithiobacillus ferrooxidans. These were structurally characterized and their activities for each reaction step were determined. In addition, the crystal structures of the wild-type SQR with sodium selenide and gold(I) cyanide have been determined. Previously we proposed a mechanism for the reduction of sulfides to elemental sulfur involving nucleophilic attack of Cys356 on C(4A) atom of FAD. Here we also consider an alternative anionic radical mechanism by direct electron transfer from Cys356 to the isoalloxazine ring of FAD.

Structure-activity characterization of sulfide:quinone oxidoreductase variants.,Cherney MM, Zhang Y, James MN, Weiner JH J Struct Biol. 2012 Apr 19. PMID:22542586[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Cherney MM, Zhang Y, James MN, Weiner JH. Structure-activity characterization of sulfide:quinone oxidoreductase variants. J Struct Biol. 2012 Apr 19. PMID:22542586 doi:10.1016/j.jsb.2012.04.007

3szc, resolution 2.20Å

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