1LM1

Structural studies on the synchronization of catalytic centers in glutamate synthase: native enzyme

1LM1 の概要

• エントリーDOI: 10.2210/pdb1lm1/pdb
• 関連するPDBエントリー: 1LLW 1LLZ
• 分子名称: Ferredoxin-dependent glutamate synthase, ACETATE ION, FLAVIN MONONUCLEOTIDE, ... (5 entities in total)
• 機能のキーワード: glutamate synthase, channeling, amidotransferase, oxidoreductase
• 由来する生物種: Synechocystis sp. PCC 6803
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 166581.92

構造登録者

van Den Heuvel, R.H.,Ferrari, D.,Bossi, R.T.,Ravasio, S.,Curti, B.,Vanoni, M.A.,Florencio, F.J.,Mattevi, A. (登録日: 2002-04-30, 公開日: 2002-07-31, 最終更新日: 2023-10-25)

主引用文献

van Den Heuvel, R.H.,Ferrari, D.,Bossi, R.T.,Ravasio, S.,Curti, B.,Vanoni, M.A.,Florencio, F.J.,Mattevi, A.
Structural studies on the synchronization of catalytic centers in glutamate synthase
J.BIOL.CHEM., 277:24579-24583, 2002

PubMed Abstract: The complex iron-sulfur flavoprotein glutamate synthase (GltS) plays a prominent role in ammonia assimilation in bacteria, yeasts, and plants. GltS catalyzes the formation of two molecules of l-glutamate from 2-oxoglutarate and l-glutamine via intramolecular channeling of ammonia. GltS has the impressive ability of synchronizing its distinct catalytic centers to avoid wasteful consumption of l-glutamine. We have determined the crystal structure of the ferredoxin-dependent GltS in several ligation and redox states. The structures reveal the crucial elements in the synchronization between the glutaminase site and the 2-iminoglutarate reduction site. The structural data combined with the catalytic properties of GltS indicate that binding of ferredoxin and 2-oxoglutarate to the FMN-binding domain of GltS induce a conformational change in the loop connecting the two catalytic centers. The rearrangement induces a shift in the catalytic elements of the amidotransferase domain, such that it becomes activated. This machinery, over a distance of more than 30 A, controls the ability of the enzyme to bind and hydrolyze the ammonia-donating substrate l-glutamine.

PubMed: 11967268
DOI: 10.1074/jbc.M202541200

実験手法

X-RAY DIFFRACTION (2.8 Å)