3h1j
From Proteopedia
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- | [[Image:3h1j.png|left|200px]] | ||
- | + | ==Stigmatellin-bound cytochrome bc1 complex from chicken== | |
+ | <StructureSection load='3h1j' size='340' side='right'caption='[[3h1j]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[3h1j]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. The May 2011 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Cytochrome bc1'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2011_5 10.2210/rcsb_pdb/mom_2011_5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H1J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3H1J 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]] 3Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CDL:CARDIOLIPIN'>CDL</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PEE:1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE'>PEE</scene>, <scene name='pdbligand=PLC:DIUNDECYL+PHOSPHATIDYL+CHOLINE'>PLC</scene>, <scene name='pdbligand=SMA:STIGMATELLIN+A'>SMA</scene>, <scene name='pdbligand=UNL:UNKNOWN+LIGAND'>UNL</scene>, <scene name='pdbligand=UQ:COENZYME+Q10,+(2Z,6E,10Z,14E,18E,22E,26Z)-ISOMER'>UQ</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=3h1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h1j OCA], [https://pdbe.org/3h1j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3h1j RCSB], [https://www.ebi.ac.uk/pdbsum/3h1j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3h1j ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/D0VX29_CHICK D0VX29_CHICK] | ||
+ | == 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/h1/3h1j_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=3h1j ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The cytochrome bc1 is one of the three major respiratory enzyme complexes residing in the inner mitochondrial membrane. Cytochrome bc1 transfers electrons from ubiquinol to cytochrome c and uses the energy thus released to form an electrochemical gradient across the inner membrane. Our X-ray crystal structures of the complex from chicken, cow and rabbit in both the presence and absence of inhibitors of quinone oxidation, reveal two different locations for the extrinsic domain of one component of the enzyme, an iron-sulphur protein. One location is close enough to the supposed quinol oxidation site to allow reduction of the Fe-S protein by ubiquinol. The other site is close enough to cytochrome c1 to allow oxidation of the Fe-S protein by the cytochrome. As neither location will allow both reactions to proceed at a suitable rate, the reaction mechanism must involve movement of the extrinsic domain of the Fe-S component in order to shuttle electrons from ubiquinol to cytochrome c1. Such a mechanism has not previously been observed in redox protein complexes. | ||
- | + | Electron transfer by domain movement in cytochrome bc1.,Zhang Z, Huang L, Shulmeister VM, Chi YI, Kim KK, Hung LW, Crofts AR, Berry EA, Kim SH Nature. 1998 Apr 16;392(6677):677-84. PMID:9565029<ref>PMID:9565029</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
+ | </div> | ||
+ | <div class="pdbe-citations 3h1j" style="background-color:#fffaf0;"></div> | ||
- | == | + | ==See Also== |
- | [[ | + | *[[Cytochrome bc1 3D structures|Cytochrome bc1 3D structures]] |
- | + | == References == | |
- | == | + | <references/> |
- | < | + | __TOC__ |
+ | </StructureSection> | ||
[[Category: Cytochrome bc1]] | [[Category: Cytochrome bc1]] | ||
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
+ | [[Category: Large Structures]] | ||
[[Category: RCSB PDB Molecule of the Month]] | [[Category: RCSB PDB Molecule of the Month]] | ||
- | + | [[Category: Berry EA]] | |
- | [[Category: Berry | + | [[Category: Chi Y-I]] |
- | [[Category: Chi | + | [[Category: Crofts AR]] |
- | [[Category: Crofts | + | [[Category: Huang L]] |
- | [[Category: Huang | + | [[Category: Hung L-W]] |
- | [[Category: Hung | + | [[Category: Kim KK]] |
- | [[Category: Kim | + | [[Category: Kim S-H]] |
- | [[Category: Kim | + | [[Category: Shulmeister VM]] |
- | [[Category: Shulmeister | + | [[Category: Zhang Z]] |
- | [[Category: Zhang | + | |
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Current revision
Stigmatellin-bound cytochrome bc1 complex from chicken
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