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3dtu

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{{Seed}}
 
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[[Image:3dtu.png|left|200px]]
 
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==Catalytic core subunits (I and II) of cytochrome c oxidase from Rhodobacter sphaeroides complexed with deoxycholic acid==
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The line below this paragraph, containing "STRUCTURE_3dtu", creates the "Structure Box" on the page.
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<StructureSection load='3dtu' size='340' side='right'caption='[[3dtu]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3dtu]] is a 4 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=3DTU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DTU FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.15&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=DMU:DECYL-BETA-D-MALTOPYRANOSIDE'>DMU</scene>, <scene name='pdbligand=DXC:(3ALPHA,5BETA,12ALPHA)-3,12-DIHYDROXYCHOLAN-24-OIC+ACID'>DXC</scene>, <scene name='pdbligand=HEA:HEME-A'>HEA</scene>, <scene name='pdbligand=HTO:HEPTANE-1,2,3-TRIOL'>HTO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=TRD:TRIDECANE'>TRD</scene></td></tr>
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{{STRUCTURE_3dtu| PDB=3dtu | SCENE= }}
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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=3dtu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dtu OCA], [https://pdbe.org/3dtu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dtu RCSB], [https://www.ebi.ac.uk/pdbsum/3dtu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dtu 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/dt/3dtu_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=3dtu ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Micromolar concentrations of the bile salt deoxycholate are shown to rescue the activity of an inactive mutant, E101A, in the K proton pathway of Rhodobacter sphaeroides cytochrome c oxidase. A crystal structure of the wild-type enzyme reveals, as predicted, deoxycholate bound with its carboxyl group at the entrance of the K path. Since cholate is a known potent inhibitor of bovine oxidase and is seen in a similar position in the bovine structure, the crystallographically defined, conserved steroid binding site could reveal a regulatory site for steroids or structurally related molecules that act on the essential K proton path.
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===Catalytic core subunits (I and II) of cytochrome c oxidase from Rhodobacter sphaeroides complexed with deoxycholic acid===
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A conserved steroid binding site in cytochrome C oxidase.,Qin L, Mills DA, Buhrow L, Hiser C, Ferguson-Miller S Biochemistry. 2008 Sep 23;47(38):9931-3. Epub 2008 Aug 30. PMID:18759498<ref>PMID:18759498</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3dtu" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_18759498}}, adds the Publication Abstract to the page
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*[[Cytochrome c oxidase 3D structures|Cytochrome c oxidase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 18759498 is the PubMed ID number.
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== References ==
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-->
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<references/>
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{{ABSTRACT_PUBMED_18759498}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Cereibacter sphaeroides]]
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3DTU 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=3DTU OCA].
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[[Category: Large Structures]]
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[[Category: Buhrow L]]
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==Reference==
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[[Category: Ferguson-Miller S]]
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A conserved steroid binding site in cytochrome C oxidase., Qin L, Mills DA, Buhrow L, Hiser C, Ferguson-Miller S, Biochemistry. 2008 Sep 23;47(38):9931-3. Epub 2008 Aug 30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18759498 18759498]
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[[Category: Hiser C]]
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[[Category: Cytochrome-c oxidase]]
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[[Category: Mills DA]]
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[[Category: Protein complex]]
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[[Category: Qin L]]
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[[Category: Rhodobacter sphaeroides]]
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[[Category: Buhrow, L.]]
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[[Category: Ferguson-Miller, S.]]
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[[Category: Hiser, C.]]
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[[Category: Mills, D A.]]
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[[Category: Qin, L.]]
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[[Category: Copper]]
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[[Category: Deoxycholic acid]]
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[[Category: Electron transport]]
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[[Category: Heme]]
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[[Category: Hydrogen ion transport]]
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[[Category: Ion transport]]
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[[Category: Iron]]
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[[Category: Membrane]]
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[[Category: Metal-binding]]
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[[Category: Oxidoreductase]]
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[[Category: Respiratory chain]]
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[[Category: Transmembrane]]
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[[Category: Transmembrane protein complex]]
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[[Category: Transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Oct 1 21:54:03 2008''
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Current revision

Catalytic core subunits (I and II) of cytochrome c oxidase from Rhodobacter sphaeroides complexed with deoxycholic acid

PDB ID 3dtu

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