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3dtu

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Revision as of 08:56, 25 October 2017

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

Structural highlights

3dtu is a 4 chain structure with sequence from "rhodococcus_capsulatus"_molisch_1907 "rhodococcus capsulatus" molisch 1907. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , , , , , , , ,
Related:	2gsm
Gene:	ctaD ("Rhodococcus capsulatus" Molisch 1907), ctaC, coxII, ctaB ("Rhodococcus capsulatus" Molisch 1907)
Activity:	Cytochrome-c oxidase, with EC number 1.9.3.1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[COX1_RHOSH] 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. [COX2_RHOSH] Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Qin L, Mills DA, Buhrow L, Hiser C, Ferguson-Miller S. A conserved steroid binding site in cytochrome C oxidase. Biochemistry. 2008 Sep 23;47(38):9931-3. Epub 2008 Aug 30. PMID:18759498 doi:10.1021/bi8013483

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3dtu"

@@ Line 1: / Line 1: @@
 ==Catalytic core subunits (I and II) of cytochrome c oxidase from Rhodobacter sphaeroides complexed with deoxycholic acid==
 <StructureSection load='3dtu' size='340' side='right' caption='[[3dtu]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ctaD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 "Rhodococcus capsulatus" Molisch 1907]), ctaC, coxII, ctaB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 "Rhodococcus capsulatus" Molisch 1907])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3dtu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dtu OCA], [http://pdbe.org/3dtu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3dtu RCSB], [http://www.ebi.ac.uk/pdbsum/3dtu PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3dtu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dtu OCA], [http://pdbe.org/3dtu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3dtu RCSB], [http://www.ebi.ac.uk/pdbsum/3dtu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3dtu ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 30: / Line 31: @@
 </div>
 <div class="pdbe-citations 3dtu" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Cytochrome c oxidase|Cytochrome c oxidase]]
 == References ==
 <references/>
@@ Line 44: / Line 42: @@
 [[Category: Mills, D A]]
 [[Category: Qin, L]]
+[[Category: Copper]]
 [[Category: Deoxycholic acid]]
 [[Category: Electron transport]]

3dtu

From Proteopedia

Revision as of 08:56, 25 October 2017

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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