1cyi

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1cyi, resolution 1.9Å

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CYTOCHROME C6

Overview

The molecular structure of cytochrome c6 from the green alga Chlamydomonas, reinhardtii has been determined from two crystal forms and refined to 1.9, A resolution. The two crystal forms are likely the result of different, levels of post-translational modification of the protein. This is the, first report of a high-resolution structure of a chloroplast-derived class, I c-type cytochrome. The overall fold is similar to that of other class I, c-type cytochromes, consisting of a series of alpha-helices and turns that, envelop the heme prosthetic group. There is also a short two-stranded, anti-parallel beta-sheet in the vicinity of the methionine axial ligand to, the heme; this region of the molecule is formed by the most highly, conserved residues in c6-type cytochromes. Although class I c-type, cytochromes are assumed to function as monomers, both crystal forms of, cytochrome c6 exhibit oligomerization about the heme crevice that is, in, part, mediated by the short anti-parallel beta-sheet. The functional, significance of this oligomerization is supported by the appearance of, similar interfaces in other electron transfer couples, HPLC and, light-scattering data, and is furthermore consistent with kinetic data on, electron transfer reactions of c6-type cytochromes.

About this Structure

1CYI is a Single protein structure of sequence from Chlamydomonas reinhardtii with CD and HEM as ligands. Full crystallographic information is available from OCA.

Reference

The structure of chloroplast cytochrome c6 at 1.9 A resolution: evidence for functional oligomerization., Kerfeld CA, Anwar HP, Interrante R, Merchant S, Yeates TO, J Mol Biol. 1995 Jul 28;250(5):627-47. PMID:7623381

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