1hh5
From Proteopedia
(Difference between revisions)
| (22 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:1hh5.gif|left|200px]]<br /> | ||
| - | <applet load="1hh5" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1hh5, resolution 1.90Å" /> | ||
| - | '''CYTOCHROME C7 FROM DESULFUROMONAS ACETOXIDANS'''<br /> | ||
| - | == | + | ==cytochrome c7 from Desulfuromonas acetoxidans== |
| - | Multihaem cytochromes play a key role in electron-transport reactions in | + | <StructureSection load='1hh5' size='340' side='right'caption='[[1hh5]], [[Resolution|resolution]] 1.90Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1hh5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Desulfuromonas_acetoxidans Desulfuromonas acetoxidans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HH5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HH5 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]] 1.9Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEC:HEME+C'>HEC</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=1hh5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hh5 OCA], [https://pdbe.org/1hh5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hh5 RCSB], [https://www.ebi.ac.uk/pdbsum/1hh5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hh5 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CYC3_DESAC CYC3_DESAC] Participates in sulfate respiration coupled with phosphorylation by transferring electrons from the enzyme dehydrogenase to ferredoxin. | ||
| + | == 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/hh/1hh5_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=1hh5 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Multihaem cytochromes play a key role in electron-transport reactions in the periplasm of sulfate- and sulfur-reducing bacteria. The redox proteins grouped in the c3 superfamily also display metal-reducing activities, which make them interesting biotechnological tools. The crystal structure of the fully oxidized cytochrome c7 from Desulfuromonas acetoxidans has been solved by combined molecular-replacement and MAD methods. The structure has been refined at 1.9 A resolution to an R value of 19.1% (R(free) = 24.3%) and includes three haems and 116 water molecules. The protein displays the cytochrome c3 fold in a highly minimized form, while haem 2 and the surrounding protein environment are missing. The geometry of haem packing and of the haem axial ligands and propionates are described and compared with that of c3 cytochromes. The crystal structure is compared with the solution structure recently obtained by NMR methods and with its homologue cytochromes of the c3 superfamily. Comparison of the high number of available structures makes it possible to analyze the structural role of the few highly conserved residues, in addition to the cysteines and histidines that link the porphyrin rings and the Fe atoms to the protein chain. | ||
| - | + | Structure of cytochrome c7 from Desulfuromonas acetoxidans at 1.9 A resolution.,Czjzek M, Arnoux P, Haser R, Shepard W Acta Crystallogr D Biol Crystallogr. 2001 May;57(Pt 5):670-8. Epub 2001, Apr 24. PMID:11320307<ref>PMID:11320307</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1hh5" style="background-color:#fffaf0;"></div> | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ==See Also== | |
| + | *[[Cytochrome C 3D structures|Cytochrome C 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Desulfuromonas acetoxidans]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Arnoux P]] | ||
| + | [[Category: Czjzek M]] | ||
| + | [[Category: Haser R]] | ||
| + | [[Category: Shepard W]] | ||
Current revision
cytochrome c7 from Desulfuromonas acetoxidans
| |||||||||||
