2dge

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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 with ZN and HEM as ligands. 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

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