This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
3t0k
From Proteopedia
(Difference between revisions)
| (4 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:3t0k.jpg|left|200px]] | ||
| - | < | + | ==Crystal structure of sulfide:quinone oxidoreductase from Acidithiobacillus ferrooxidans with bound trisulfide and decylubiquinone== |
| - | + | <StructureSection load='3t0k' size='340' side='right'caption='[[3t0k]], [[Resolution|resolution]] 2.00Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3t0k]] 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=3T0K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T0K FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=S3H:TRISULFANE'>S3H</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"><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]], [[3szc|3szc]], [[3szf|3szf]], [[3szw|3szw]], [[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 ([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'>[https://proteopedia.org/fgij/fg.htm?mol=3t0k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t0k OCA], [https://pdbe.org/3t0k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t0k RCSB], [https://www.ebi.ac.uk/pdbsum/3t0k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t0k ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:22542586</ref> | |
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 3t0k" style="background-color:#fffaf0;"></div> | ||
| - | + | ==See Also== | |
| - | + | *[[Quinone reductase|Quinone reductase]] | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | == | + | [[Category: Acif2]] |
| - | [[ | + | [[Category: Large Structures]] |
| - | + | [[Category: Cherney, M M]] | |
| - | == | + | [[Category: James, M N.G]] |
| - | < | + | [[Category: Weiner, J H]] |
| - | [[Category: | + | [[Category: Zhang, Y]] |
| - | [[Category: Cherney, M M | + | |
| - | [[Category: James, M N.G | + | |
| - | [[Category: Weiner, J H | + | |
| - | [[Category: Zhang, Y | + | |
[[Category: Complex with tetrasulfur and decylubiquinone]] | [[Category: Complex with tetrasulfur and decylubiquinone]] | ||
[[Category: Integral monotopic membrane protein]] | [[Category: Integral monotopic membrane protein]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
[[Category: Sulfide:quinone oxidoreductase]] | [[Category: Sulfide:quinone oxidoreductase]] | ||
Current revision
Crystal structure of sulfide:quinone oxidoreductase from Acidithiobacillus ferrooxidans with bound trisulfide and decylubiquinone
| |||||||||||
