3h8l
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3h8l is ON HOLD Authors: Brito, Jose A. Description: The first X-ray structure of sulfide:quinone oxidoreductase: insights into sulfide oxidation m...) |
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- | '''Unreleased structure''' | ||
- | The | + | ==The first X-ray structure of a sulfide:quinone oxidoreductase: insights into sulfide oxidation mechanism== |
+ | <StructureSection load='3h8l' size='340' side='right'caption='[[3h8l]], [[Resolution|resolution]] 2.57Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[3h8l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acidianus_ambivalens Acidianus ambivalens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H8L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3H8L 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]] 2.57Å</td></tr> | ||
+ | <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=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=S3H:TRISULFANE'>S3H</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=3h8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h8l OCA], [https://pdbe.org/3h8l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3h8l RCSB], [https://www.ebi.ac.uk/pdbsum/3h8l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3h8l ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/SQRD_ACIAM SQRD_ACIAM] Catalyzes the oxidation of sulfides, such as hydrogen sulfide, with the help of a quinone. Has the highest activity with caldariella quinone and decylubiquinone, and lower activity with naphtoquinones. 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:19438211</ref> | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h8/3h8l_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3h8l ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | A sulfide:quinone oxidoreductase (SQR) was isolated from the membranes of the hyperthermoacidophilic archaeon Acidianus ambivalens, and its X-ray structure, the first reported for an SQR, was determined to 2.6 A resolution. This enzyme was functionally and structurally characterized and was shown to have two redox active sites: a covalently bound FAD and an adjacent pair of cysteine residues. Most interestingly, the X-ray structure revealed the presence of a chain of three sulfur atoms bridging those two cysteine residues. The possible implications of this observation in the catalytic mechanism for sulfide oxidation are discussed, and the role of SQR in the sulfur dependent bioenergetics of A. ambivalens, linked to oxygen reduction, is addressed. | ||
- | + | Structural and functional insights into sulfide:quinone oxidoreductase.,Brito JA, Sousa FL, Stelter M, Bandeiras TM, Vonrhein C, Teixeira M, Pereira MM, Archer M Biochemistry. 2009 Jun 23;48(24):5613-22. PMID:19438211<ref>PMID:19438211</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
+ | </div> | ||
+ | <div class="pdbe-citations 3h8l" style="background-color:#fffaf0;"></div> | ||
- | + | ==See Also== | |
+ | *[[Quinone reductase 3D structures|Quinone reductase 3D structures]] | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Acidianus ambivalens]] | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Archer M]] | ||
+ | [[Category: Bandeiras TM]] | ||
+ | [[Category: Brito JA]] | ||
+ | [[Category: Pereira MM]] | ||
+ | [[Category: Sousa FL]] | ||
+ | [[Category: Stelter M]] | ||
+ | [[Category: Teixeira M]] | ||
+ | [[Category: Vonrhein C]] |
Current revision
The first X-ray structure of a sulfide:quinone oxidoreductase: insights into sulfide oxidation mechanism
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