Structural highlights
3x2q is a 20 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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Method: | X-ray diffraction, Resolution 2Å |
Ligands: | , , , , , , , , , , , , , , , , , |
Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
COX1_BOVIN 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.
Publication Abstract from PubMed
The X-ray structure of cyanide-bound bovine heart cytochrome c oxidase in the fully oxidized state was determined at 2.0 A resolution. The structure reveals that the peroxide that bridges the two metals in the fully oxidized state is replaced by a cyanide ion bound in a nearly symmetric end-on fashion without significantly changing the protein conformation outside the two metal sites.
X-ray structure of cyanide-bound bovine heart cytochrome c oxidase in the fully oxidized state at 2.0 A resolution.,Yano N, Muramoto K, Mochizuki M, Shinzawa-Itoh K, Yamashita E, Yoshikawa S, Tsukihara T Acta Crystallogr F Struct Biol Commun. 2015 Jun;71(Pt 6):726-30. doi:, 10.1107/S2053230X15007025. Epub 2015 May 22. PMID:26057802[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Yano N, Muramoto K, Mochizuki M, Shinzawa-Itoh K, Yamashita E, Yoshikawa S, Tsukihara T. X-ray structure of cyanide-bound bovine heart cytochrome c oxidase in the fully oxidized state at 2.0 A resolution. Acta Crystallogr F Struct Biol Commun. 2015 Jun;71(Pt 6):726-30. doi:, 10.1107/S2053230X15007025. Epub 2015 May 22. PMID:26057802 doi:http://dx.doi.org/10.1107/S2053230X15007025