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|3dtu, resolution 2.15Å ()|
|Ligands:||, , , , , , , , , ,|
|Gene:||ctaD (Rhodobacter sphaeroides), ctaC, coxII, ctaB (Rhodobacter sphaeroides)|
Catalytic core subunits (I and II) of cytochrome c oxidase from Rhodobacter sphaeroides complexed with deoxycholic acid
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.