Absolute configuration of the hydroxyfarnesylethyl group of haem A, determined by X-ray structural analysis of bovine heart cytochrome c oxidase using methods applicable at 2.8 Angstrom resolution.
The absolute configuration of haem A, the prosthetic group of cytochrome c oxidase, was determined to be S by analysis of the bond angles surrounding the chiral centre of haem A after refinement with X-PLOR starting from respective initial structures with R and S configurations under absolute configuration constraints at 1.8 Angstrom resolution. The same result was obtained by refinement at 1.8 Angstrom resolution without the absolute configuration constraints. Both of these methods were applicable down to a resolution of about 2.8 Angstrom. The constrained refinement converges more quickly than the unconstrained refinement.
Yamashita
Eiki
E
Institute for Protein Research, Osaka University, 3-2 Yamada-oka, Suita 565-0871, Japan.
Aoyama
Hiroshi
H
Yao
Min
M
Muramoto
Kazumasa
K
Shinzawa-Itoh
Kyoko
K
Yoshikawa
Shinya
S
Tsukihara
Tomitake
T
D000818:Animals; D002417:Cattle; D018360:Crystallography, X-Ray / Q000379:methods*; D003576:Electron Transport Complex IV / Q000737:chemistry*; D004583:Electrons; D006418:Heme / Q000031:analogs & derivatives* / Q000737:chemistry; D008956:Models, Chemical; D008958:Models, Molecular; D008968:Molecular Conformation; D009206:Myocardium / Q000378:metabolism*; D011487:Protein Conformation; D012984:Software
C027728:heme a; D006418:Heme; D003576:Electron Transport Complex IV