5H8Y

Crystal structure of the complex between maize sulfite reductase and ferredoxin in the form-2 crystal

5H8Y の概要

• エントリーDOI: 10.2210/pdb5h8y/pdb
• 関連するPDBエントリー: 3B2F 5H8V 5H92
• 分子名称: Sulfite reductase [ferredoxin], chloroplastic, Ferredoxin-1, chloroplastic, IRON/SULFUR CLUSTER, ... (8 entities in total)
• 機能のキーワード: ferredoxin, sulfite reductase, oxidoreductase-electron transport complex, oxidoreductase/electron transport
• 由来する生物種: Zea mays (Maize); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 287012.19

構造登録者

Kurisu, G.,Nakayama, M.,Hase, T. (登録日: 2015-12-25, 公開日: 2016-04-13, 最終更新日: 2024-11-13)

主引用文献

Kim, J.Y.,Nakayama, M.,Toyota, H.,Kurisu, G.,Hase, T.
Structural and mutational studies of an electron transfer complex of maize sulfite reductase and ferredoxin.
J.Biochem., 160:101-109, 2016

PubMed Abstract: The structure of the complex of maize sulfite reductase (SiR) and ferredoxin (Fd) has been determined by X-ray crystallography. Co-crystals of the two proteins prepared under different conditions were subjected to the diffraction analysis and three possible structures of the complex were solved. Although topological relationship of SiR and Fd varied in each of the structures, two characteristics common to all structures were found in the pattern of protein-protein interactions and positional arrangements of redox centres; (i) a few negative residues of Fd contact with a narrow area of SiR with positive electrostatic surface potential and (ii) [2Fe-2S] cluster of Fd and [4Fe-4S] cluster of SiR are in a close proximity with the shortest distance around 12 Å. Mutational analysis of a total of seven basic residues of SiR distributed widely at the interface of the complex showed their importance for supporting an efficient Fd-dependent activity and a strong physical binding to Fd. These combined results suggest that the productive electron transfer complex of SiR and Fd could be formed through multiple processes of the electrostatic intermolecular interaction and this implication is discussed in terms of the multi-functionality of Fd in various redox metabolisms.

PubMed: 26920048
DOI: 10.1093/jb/mvw016

実験手法

X-RAY DIFFRACTION (2.2 Å)