5AUK

Crystal structure of the Ga-substituted Ferredoxin

5AUK の概要

• エントリーDOI: 10.2210/pdb5auk/pdb
• 関連するPDBエントリー: 5AUI
• 分子名称: Ferredoxin-1, [2Ga-2S] cluster, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: analogue, electron transfer protein, electron transport
• 由来する生物種: Synechocystis sp. (strain PCC 6803 / Kazusa)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11353.65

構造登録者

Kurisu, G.,Muraki, N.,Taya, M.,Hase, T. (登録日: 2015-04-24, 公開日: 2015-09-23, 最終更新日: 2023-11-08)

主引用文献

Mutoh, R.,Muraki, N.,Shinmura, K.,Kubota-Kawai, H.,Lee, Y.H.,Nowaczyk, M.M.,Rogner, M.,Hase, T.,Ikegami, T.,Kurisu, G.
X-ray Structure and Nuclear Magnetic Resonance Analysis of the Interaction Sites of the Ga-Substituted Cyanobacterial Ferredoxin
Biochemistry, 54:6052-6061, 2015

PubMed Abstract: In chloroplasts, ferredoxin (Fd) is reduced by Photosystem I (PSI) and oxidized by Fd-NADP(+) reductase (FNR) that is involved in NADP(+) reduction. To understand the structural basis for the dynamics and efficiency of the electron transfer reaction via Fd, we complementary used X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy. In the NMR analysis of the formed electron transfer complex with Fd, the paramagnetic effect of the [2Fe-2S] cluster of Fd prevented us from detecting the NMR signals around the cluster. To solve this problem, the paramagnetic iron-sulfur cluster was replaced with a diamagnetic metal cluster. We determined the crystal structure of the Ga-substituted Fd (GaFd) from Synechocystis sp. PCC6803 at 1.62 Å resolution and verified its functional complementation using affinity chromatography. NMR analysis of the interaction sites on GaFd with PSI (molecular mass of ∼1 MDa) and FNR from Thermosynechococcus elongatus was achieved with high-field NMR spectroscopy. With reference to the interaction sites with FNR of Anabaena sp. PCC 7119 from the published crystal data, the interaction sites of Fd with FNR and PSI in solution can be classified into two types: (1) the core hydrophobic residues in the proximity of the metal center and (2) the hydrophilic residues surrounding the core. The former sites are shared in the Fd:FNR and Fd:PSI complex, while the latter ones are target-specific and not conserved on the residual level.

PubMed: 26348494
DOI: 10.1021/acs.biochem.5b00601

実験手法

X-RAY DIFFRACTION (1.62 Å)