3dtu | pdb_00003dtu

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

spinqualitylabelsall models 3dtu, resolution 2.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D 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: CA, CD, CU, DMU, DXC, HEA, HTO, MG, OH, PO4, TRD 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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