3A9F

Crystal structure of the C-terminal domain of cytochrome cz from Chlorobium tepidum

3A9F の概要

• エントリーDOI: 10.2210/pdb3a9f/pdb
• 分子名称: Cytochrome c, HEME C, SODIUM ION, ... (8 entities in total)
• 機能のキーワード: alpha helix, cytochrome, mono heme, electron transport
• 由来する生物種: Chlorobaculum tepidum
• 細胞内の位置: Cell inner membrane ; Multi-pass membrane protein : O07091
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 22310.21

構造登録者

Hirano, Y.,Higuchi, M.,Azai, C.,Oh-oka, H.,Miki, K.,Wang, Z.-Y. (登録日: 2009-10-25, 公開日: 2010-03-02, 最終更新日: 2024-03-13)

主引用文献

Hirano, Y.,Higuchi, M.,Azai, C.,Oh-Oka, H.,Miki, K.,Wang, Z.-Y.
Crystal structure of the electron carrier domain of the reaction center cytochrome c(z) subunit from green photosynthetic bacterium Chlorobium tepidum
J.Mol.Biol., 397:1175-1187, 2010

PubMed Abstract: In green sulfur photosynthetic bacteria, the cytochrome c(z) (cyt c(z)) subunit in the reaction center complex mediates electron transfer mainly from menaquinol/cytochrome c oxidoreductase to the special pair (P840) of the reaction center. The cyt c(z) subunit consists of an N-terminal transmembrane domain and a C-terminal soluble domain that binds a single heme group. The periplasmic soluble domain has been proposed to be highly mobile and to fluctuate between oxidoreductase and P840 during photosynthetic electron transfer. We have determined the crystal structure of the oxidized form of the C-terminal functional domain of the cyt c(z) subunit (C-cyt c(z)) from thermophilic green sulfur bacterium Chlorobium tepidum at 1.3-A resolution. The overall fold of C-cyt c(z) consists of four alpha-helices and is similar to that of class I cytochrome c proteins despite the low similarity in their amino acid sequences. The N-terminal structure of C-cyt c(z) supports the swinging mechanism previously proposed in relation with electron transfer, and the surface properties provide useful information on possible interaction sites with its electron transfer partners. Several characteristic features are observed for the heme environment: These include orientation of the axial ligands with respect to the heme plane, surface-exposed area of the heme, positions of water molecules, and hydrogen-bond network involving heme propionate groups. These structural features are essential for elucidating the mechanism for regulating the redox state of cyt c(z).

PubMed: 20156447
DOI: 10.1016/j.jmb.2010.02.011

実験手法

X-RAY DIFFRACTION (1.3 Å)