2dge
From Proteopedia
Crystal structure of oxidized cytochrome C6A from Arabidopsis thaliana
Overview
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.
About this Structure
2DGE is a Single protein structure of sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.
Reference
Crystal structure of oxidized cytochrome c(6A) from Arabidopsis thaliana., 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, FEBS Lett. 2006 Jun 26;580(15):3763-8. Epub 2006 Jun 9. PMID:16777100 Page seeded by OCA on Sun May 4 00:22:16 2008
Categories: Arabidopsis thaliana | Single protein | Akazaki, H. | Chida, H. | Hirano, T. | Kawachi, R. | Kawai, F. | Nakazawa, A. | Nishio, T. | Oku, T. | Park, S Y. | Satoh, T. | Suruga, K. | Takayama, Y. | Unzai, S. | Yamada, S. | Yokoyama, T. | Crystal structure | Cytochrome c6a | Electron transfer | Heme exposure
