3W5V

Cross-linked complex between Ferredoxin and Ferredoxin-NADP+ reductase

3W5V の概要

• エントリーDOI: 10.2210/pdb3w5v/pdb
• 関連するPDBエントリー: 1GAW 3B2F 3W5U
• 分子名称: Ferredoxin, Ferredoxin-1, chloroplastic, FLAVIN-ADENINE DINUCLEOTIDE, ... (4 entities in total)
• 機能のキーワード: electron transfer complex, electron transport
• 由来する生物種: Zea mays (maize); 詳細
• 細胞内の位置: Plastid, chloroplast: P27787
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 93692.56

構造登録者

Kimata-Ariga, Y.,Kubota-Kawai, H.,Muraki, N.,Hase, T.,Kurisu, G. (登録日: 2013-02-06, 公開日: 2013-06-19, 最終更新日: 2024-10-30)

主引用文献

Kimata-Ariga, Y.,Kubota-Kawai, H.,Lee, Y.-H.,Muraki, N.,Ikegami, T.,Kurisu, G.,Hase, T.
Concentration-dependent oligomerization of cross-linked complexes between ferredoxin and ferredoxin-NADP(+) reductase
Biochem.Biophys.Res.Commun., 434:867-872, 2013

PubMed Abstract: Ferredoxin-NADP(+) reductase (FNR) forms a 1:1 complex with ferredoxin (Fd), and catalyzes the electron transfer between Fd and NADP(+). In our previous study, we prepared a series of site-specifically cross-linked complexes of Fd and FNR, which showed diverse electron transfer properties. Here, we show that X-ray crystal structures of the two different Fd-FNR cross-linked complexes form oligomers by swapping Fd and FNR moieties across the molecules; one complex is a dimer from, and the other is a successive multimeric form. In order to verify whether these oligomeric structures are formed only in crystal, we investigated the possibility of the oligomerization of these complexes in solution. The mean values of the particle size of these cross-linked complexes were shown to increase with the rise of protein concentration at sub-milimolar order, whereas the size of dissociable wild-type Fd:FNR complex was unchanged as analyzed by dynamic light scattering measurement. The oligomerization products were detected by SDS-PAGE after chemical cross-linking of these complexes at the sub-milimolar concentrations. The extent and concentration-dependent profile of the oligomerizaion were differentiated between the two cross-linked complexes. These results show that these Fd-FNR cross-linked complexes exhibit concentration-dependent oligomerization, possibly through swapping of Fd and FNR moieties also in solution. These findings lead to the possibility that some native multi-domain proteins may present similar phenomenon in vivo.

PubMed: 23618857
DOI: 10.1016/j.bbrc.2013.04.033

実験手法

X-RAY DIFFRACTION (3.81 Å)