RRC ID 1881
Author Chida H, Yokoyama T, Kawai F, Nakazawa A, Akazaki H, Takayama Y, Hirano T, Suruga K, Satoh T, Yamada S, Kawachi R, Unzai S, Nishio T, Park SY, Oku T.
Title Crystal structure of oxidized cytochrome c(6A) from Arabidopsis thaliana.
Journal FEBS Lett
Abstract Compared with algal and cyanobacterial cytochrome c(6), cytochrome c(6A) from higher plants contains an additional loop of 12 amino acid residues. We have determined the first crystal structure of cytochrome c(6A) from Arabidopsis thaliana at 1.5 Angstrom resolution in order to help elucidate its function. The overall structure of cytochrome c(6A) follows the topology of class I c-type cytochromes in which the heme prosthetic group covalently binds to Cys16 and Cys19, and the iron has octahedral coordination with His20 and Met60 as the axial ligands. Two cysteine residues (Cys67 and Cys73) within the characteristic 12 amino acids loop form a disulfide bond, contributing to the structural stability of cytochrome c(6A). Our model provides a chemical basis for the known low redox potential of cytochrome c(6A) which makes it an unsuitable electron carrier between cytochrome b(6)f and PSI.
Volume 580(15)
Pages 3763-8
Published 2006-6-26
DOI 10.1016/j.febslet.2006.05.067
PII S0014-5793(06)00684-3
PMID 16777100
MeSH Arabidopsis / enzymology* Arabidopsis Proteins / chemistry* Arabidopsis Proteins / genetics Binding Sites Crystallography, X-Ray Cysteine / genetics Cysteine / metabolism Cytochromes c6 / chemistry* Cytochromes c6 / genetics Cytochromes c6 / metabolism Heme Models, Molecular Oxidation-Reduction Protein Structure, Tertiary Structural Homology, Protein
IF 3.057
Times Cited 13
WOS Category BIOPHYSICS BIOCHEMISTRY & MOLECULAR BIOLOGY CELL BIOLOGY
Resource
Arabidopsis / Cultured plant cells, genes pda02263