1F1F

CRYSTAL STRUCTURE OF CYTOCHROME C6 FROM ARTHROSPIRA MAXIMA

1F1F の概要

• エントリーDOI: 10.2210/pdb1f1f/pdb
• 関連するPDBエントリー: 1CYI
• 分子名称: CYTOCHROME C6, HEME C (2 entities in total)
• 機能のキーワード: cytochrome c6, heme, protein structure, cyanobacteria, photosynthesis, electron transport
• 由来する生物種: Arthrospira maxima
• 細胞内の位置: Cellular thylakoid lumen : P00118
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9848.85

構造登録者

Kerfeld, C.A.,Serag, A.A.,Sawaya, M.R.,Krogmann, D.W.,Yeates, T.O. (登録日: 2000-05-18, 公開日: 2001-08-08, 最終更新日: 2021-03-03)

主引用文献

Sawaya, M.R.,Krogmann, D.W.,Serag, A.,Ho, K.K.,Yeates, T.O.,Kerfeld, C.A.
Structures of cytochrome c-549 and cytochrome c6 from the cyanobacterium Arthrospira maxima.
Biochemistry, 40:9215-9225, 2001

PubMed Abstract: Cytochrome c(6) and cytochrome c-549 are small (89 and 130 amino acids, respectively) monoheme cytochromes that function in photosynthesis. They appear to have descended relatively recently from the same ancestral gene but have diverged to carry out very different functional roles, underscored by the large difference between their midpoint potentials of nearly 600 mV. We have determined the X-ray crystal structures of both proteins isolated from the cyanobacterium Arthrospira maxima. The two structures are remarkably similar, superimposing on backbone atoms with an rmsd of 0.7 A. Comparison of the two structures suggests that differences in solvent exposure of the heme and the electrostatic environment of the heme propionates, as well as in heme iron ligation, are the main determinants of midpoint potential in the two proteins. In addition, the crystal packing of both A. maxima cytochrome c-549 and cytochrome c(6) suggests that the proteins oligomerize. Finally, the cytochrome c-549 dimer we observe can be readily fit into the recently described model of cyanobacterial photosystem II.

PubMed: 11478889
DOI: 10.1021/bi002679p

実験手法

X-RAY DIFFRACTION (2.7 Å)