3DTU

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

Summary for 3DTU

• Entry DOI: 10.2210/pdb3dtu/pdb
• Related: 2GSM
• Descriptor: Cytochrome c oxidase subunit 1, TRIDECANE, CADMIUM ION, ... (14 entities in total)
• Functional Keywords: transmembrane protein complex, deoxycholic acid, copper, electron transport, heme, hydrogen ion transport, ion transport, iron, membrane, metal-binding, oxidoreductase, respiratory chain, transmembrane, transport
• Biological source: Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides); More
• Cellular location: Cell membrane; Multi-pass membrane protein: P33517 Q03736
• Total number of polymer chains: 4
• Total formula weight: 198953.07

Authors

Qin, L.,Mills, D.A.,Buhrow, L.,Hiser, C.,Ferguson-Miller, S. (deposition date: 2008-07-15, release date: 2008-09-16, Last modification date: 2024-10-09)

Primary citation

Qin, L.,Mills, D.A.,Buhrow, L.,Hiser, C.,Ferguson-Miller, S.
A conserved steroid binding site in cytochrome C oxidase.
Biochemistry, 47:9931-9933, 2008

PubMed Abstract: 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.

PubMed: 18759498
DOI: 10.1021/bi8013483

Experimental method

X-RAY DIFFRACTION (2.15 Å)