1KDJ

OXIDIZED FORM OF PLASTOCYANIN FROM DRYOPTERIS CRASSIRHIZOMA

1KDJ の概要

• エントリーDOI: 10.2210/pdb1kdj/pdb
• 分子名称: PLASTOCYANIN, COPPER (II) ION (3 entities in total)
• 機能のキーワード: electron transfer, photosystem, pai-pai stacking
• 由来する生物種: Adiantum capillus-veneris
• 細胞内の位置: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein; Lumenal side: Q7SIB8
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10849.52

構造登録者

Inoue, T.,Gotowda, M.,Hamada, K.,Kohzuma, T.,Yoshizaki, F.,Sugimura, Y.,Kai, Y. (登録日: 1998-05-08, 公開日: 1999-05-11, 最終更新日: 2024-04-03)

主引用文献

Kohzuma, T.,Inoue, T.,Yoshizaki, F.,Sasakawa, Y.,Onodera, K.,Nagatomo, S.,Kitagawa, T.,Uzawa, S.,Isobe, Y.,Sugimura, Y.,Gotowda, M.,Kai, Y.
The structure and unusual pH dependence of plastocyanin from the fern Dryopteris crassirhizoma. The protonation of an active site histidine is hindered by pi-pi interactions.
J.Biol.Chem., 274:11817-11823, 1999

PubMed Abstract: Spectroscopic properties, amino acid sequence, electron transfer kinetics, and crystal structures of the oxidized (at 1.7 A resolution) and reduced form (at 1.8 A resolution) of a novel plastocyanin from the fern Dryopteris crassirhizoma are presented. Kinetic studies show that the reduced form of Dryopteris plastocyanin remains redox-active at low pH, under conditions where the oxidation of the reduced form of other plastocyanins is inhibited by the protonation of a solvent-exposed active site residue, His87 (equivalent to His90 in Dryopteris plastocyanin). The x-ray crystal structure analysis of Dryopteris plastocyanin reveals pi-pi stacking between Phe12 and His90, suggesting that the active site is uniquely protected against inactivation. Like higher plant plastocyanins, Dryopteris plastocyanin has an acidic patch, but this patch is located closer to the solvent-exposed active site His residue, and the total number of acidic residues is smaller. In the reactions of Dryopteris plastocyanin with inorganic redox reagents, the acidic patch (the "remote" site) and the hydrophobic patch surrounding His90 (the "adjacent" site) are equally efficient for electron transfer. These results indicate the significance of the lack of protonation at the active site of Dryopteris plastocyanin, the equivalence of the two electron transfer sites in this protein, and a possibility of obtaining a novel insight into the photosynthetic electron transfer system of the first vascular plant fern, including its molecular evolutionary aspects. This is the first report on the characterization of plastocyanin and the first three-dimensional protein structure from fern plant.

PubMed: 10206999
DOI: 10.1074/jbc.274.17.11817

実験手法

X-RAY DIFFRACTION (1.7 Å)