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1m56

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[[Image:1m56.gif|left|200px]]
 
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{{Structure
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==Structure of cytochrome c oxidase from Rhodobactor sphaeroides (Wild Type)==
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|PDB= 1m56 |SIZE=350|CAPTION= <scene name='initialview01'>1m56</scene>, resolution 2.3&Aring;
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<StructureSection load='1m56' size='340' side='right'caption='[[1m56]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HEA:HEME-A'>HEA</scene> and <scene name='pdbligand=PEH:DI-STEAROYL-3-SN-PHOSPHATIDYLETHANOLAMINE'>PEH</scene>
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<table><tr><td colspan='2'>[[1m56]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Cereibacter_sphaeroides Cereibacter sphaeroides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M56 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M56 FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Cytochrome-c_oxidase Cytochrome-c oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.9.3.1 1.9.3.1]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3PE:1,2-DIACYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE'>3PE</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=HEA:HEME-A'>HEA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1m56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m56 OCA], [https://pdbe.org/1m56 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m56 RCSB], [https://www.ebi.ac.uk/pdbsum/1m56 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m56 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/COX1_CERSP COX1_CERSP] Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Co I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme a of subunit 1 to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m5/1m56_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1m56 ConSurf].
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<div style="clear:both"></div>
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'''Structure of cytochrome c oxidase from Rhodobactor sphaeroides (Wild Type)'''
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==See Also==
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*[[Cytochrome c oxidase 3D structures|Cytochrome c oxidase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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The structure of cytochrome c oxidase from Rhodobacter sphaeroides has been solved at 2.3/2.8A (anisotropic resolution). This high-resolution structure revealed atomic details of a bacterial terminal oxidase including water molecule positions and a potential oxygen pathway, which has not been reported in other oxidase structures. A comparative study of the wild-type and the EQ(I-286) mutant enzyme revealed structural rearrangements around E(I-286) that could be crucial for proton transfer in this enzyme. In the structure of the mutant enzyme, EQ(I-286), which cannot transfer protons during oxygen reduction, the side-chain of Q(I-286) does not have the hydrogen bond to the carbonyl oxygen of M(I-107) that is seen in the wild-type structure. Furthermore, the Q(I-286) mutant has a different arrangement of water molecules and residues in the vicinity of the Q side-chain. These differences between the structures could reflect conformational changes that take place upon deprotonation of E(I-286) during turnover of the wild-type enzyme, which could be part of the proton-pumping machinery of the enzyme.
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[[Category: Cereibacter sphaeroides]]
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[[Category: Large Structures]]
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==About this Structure==
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[[Category: Abramson J]]
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1M56 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M56 OCA].
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[[Category: Brezezinski P]]
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[[Category: Iwata S]]
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==Reference==
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[[Category: Larsson G]]
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The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides., Svensson-Ek M, Abramson J, Larsson G, Tornroth S, Brzezinski P, Iwata S, J Mol Biol. 2002 Aug 9;321(2):329-39. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12144789 12144789]
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[[Category: Svensson-Ek M]]
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[[Category: Cytochrome-c oxidase]]
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[[Category: Tornroth S]]
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[[Category: Protein complex]]
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[[Category: Rhodobacter sphaeroides]]
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[[Category: Abramson, J.]]
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[[Category: Brezezinski, P.]]
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[[Category: Iwata, S.]]
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[[Category: Larsson, G.]]
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[[Category: Svensson-Ek, M.]]
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[[Category: Tornroth, S.]]
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[[Category: CA]]
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[[Category: CU]]
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[[Category: HEA]]
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[[Category: MG]]
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[[Category: PEH]]
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[[Category: membrane protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:39:00 2008''
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Current revision

Structure of cytochrome c oxidase from Rhodobactor sphaeroides (Wild Type)

PDB ID 1m56

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