1CYI

CYTOCHROME C6

1CYI の概要

• エントリーDOI: 10.2210/pdb1cyi/pdb
• 分子名称: CYTOCHROME C6, CADMIUM ION, HEME C, ... (4 entities in total)
• 機能のキーワード: photosynthesis, chlamydomonas, electron transport protein (cytochrome)
• 由来する生物種: Chlamydomonas reinhardtii
• 細胞内の位置: Plastid, chloroplast thylakoid lumen: P08197
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10879.14

構造登録者

Kerfeld, C.A.,Yeates, T.O. (登録日: 1995-05-09, 公開日: 1996-01-29, 最終更新日: 2024-10-30)

主引用文献

Kerfeld, C.A.,Anwar, H.P.,Interrante, R.,Merchant, S.,Yeates, T.O.
The structure of chloroplast cytochrome c6 at 1.9 A resolution: evidence for functional oligomerization.
J.Mol.Biol., 250:627-647, 1995

PubMed Abstract: 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.

PubMed: 7623381
DOI: 10.1006/jmbi.1995.0404

実験手法

X-RAY DIFFRACTION (1.9 Å)