1EYS

CRYSTAL STRUCTURE OF PHOTOSYNTHETIC REACTION CENTER FROM A THERMOPHILIC BACTERIUM, THERMOCHROMATIUM TEPIDUM

1EYS の概要

• エントリーDOI: 10.2210/pdb1eys/pdb
• 分子名称: PHOTOSYNTHETIC REACTION CENTER, FE (III) ION, MENAQUINONE 8, ... (14 entities in total)
• 機能のキーワード: membrane protein complex, electron transport
• 由来する生物種: Thermochromatium tepidum; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 148848.86

構造登録者

Nogi, T.,Fathir, I.,Kobayashi, M.,Nozawa, T.,Miki, K. (登録日: 2000-05-08, 公開日: 2000-12-13, 最終更新日: 2024-10-09)

主引用文献

Nogi, T.,Fathir, I.,Kobayashi, M.,Nozawa, T.,Miki, K.
Crystal structures of photosynthetic reaction center and high-potential iron-sulfur protein from Thermochromatium tepidum: thermostability and electron transfer.
Proc.Natl.Acad.Sci.USA, 97:13561-13566, 2000

PubMed Abstract: The reaction center (RC) of photosynthetic bacteria is a membrane protein complex that promotes a light-induced charge separation during the primary process of photosynthesis. In the photosynthetic electron transfer chain, the soluble electron carrier proteins transport electrons to the RC and reduce the photo-oxidized special-pair of bacteriochlorophyll. The high-potential iron-sulfur protein (HiPIP) is known to serve as an electron donor to the RC in some species, where the c-type cytochrome subunit, the peripheral subunit of the RC, directly accepts electrons from the HiPIP. Here we report the crystal structures of the RC and the HiPIP from Thermochromatium (Tch.) tepidum, at 2.2-A and 1.5-A resolution, respectively. Tch. tepidum can grow at the highest temperature of all known purple bacteria, and the Tch. tepidum RC shows some degree of stability to high temperature. Comparison with the RCs of mesophiles, such as Blastochloris viridis, has shown that the Tch. tepidum RC possesses more Arg residues at the membrane surface, which might contribute to the stability of this membrane protein. The RC and the HiPIP both possess hydrophobic patches on their respective surfaces, and the HiPIP is expected to interact with the cytochrome subunit by hydrophobic interactions near the heme-1, the most distal heme to the special-pair.

PubMed: 11095707
DOI: 10.1073/pnas.240224997

実験手法

X-RAY DIFFRACTION (2.2 Å)