Reference - Detail
RRC ID | 1881 |
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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 |