1IWA

RUBISCO FROM GALDIERIA PARTITA

1IWA の概要

• エントリーDOI: 10.2210/pdb1iwa/pdb
• 関連するPDBエントリー: 1BWV 1EJ7 1IR1
• 分子名称: ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit, ribulose-1,5-bisphosphate carboxylase/oxygenase small subunit, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: rubisco, photosynthesis, lyase
• 由来する生物種: Galdieria partita; 詳細
• 細胞内の位置: Plastid, chloroplast (By similarity): O98949
• タンパク質・核酸の鎖数: 16
• 化学式量合計: 570930.36

構造登録者

Okano, Y.,Mizohata, E.,Xie, Y.,Matsumura, H.,Sugawara, H.,Inoue, T.,Yokota, A.,Kai, Y. (登録日: 2002-04-30, 公開日: 2003-04-30, 最終更新日: 2023-12-27)

主引用文献

Okano, Y.,Mizohata, E.,Xie, Y.,Matsumura, H.,Sugawara, H.,Inoue, T.,Yokota, A.,Kai, Y.
X-Ray Structure of Galdieria Rubisco Complexed with one sulfate ion per active site
FEBS LETT., 527:33-36, 2002

PubMed Abstract: Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) catalyzes the reactions of carboxylation and oxygenation of ribulose-1,5-bisphosphate. These reactions require that the active site should be closed by a flexible loop (loop 6) of the large subunit. Rubisco from a red alga, Galdieria partita, has the highest specificity for carboxylation reaction among the Rubiscos hitherto reported. The crystal structure of unactivated Galdieria Rubisco has been determined at 2.6 A resolution. The electron density map reveals that a sulfate binds only to the P1 anion-binding site of the active site and the loop 6 is closed. Galdieria Rubisco has a unique hydrogen bond between the main chain oxygen of Val332 on the loop 6 and the epsilon-amino group of Gln386 of the same large subunit. This interaction is likely to be crucial to understanding for stabilizing the loop 6 in the closed state and to making a higher affinity for anionic ligands.

PubMed: 12220629
DOI: 10.1016/S0014-5793(02)03148-4

実験手法

X-RAY DIFFRACTION (2.6 Å)