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 Rhodobacter sphaeroides. 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 (Rhodobacter sphaeroides), ctaC, coxII, ctaB (Rhodobacter sphaeroides) Activity: Cytochrome-c oxidase, with EC number 1.9.3.1 Resources: FirstGlance, OCA, RCSB, PDBsum 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. See Also Cytochrome c oxidase

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