5GUD

Glutamate dehydrogenase from Corynebacterium glutamicum (alpha-iminoglutarate/NADP+ complex)

5GUD の概要

• エントリーDOI: 10.2210/pdb5gud/pdb
• 分子名称: Glutamate dehydrogenase, (2Z)-2-iminopentanedioic acid, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (6 entities in total)
• 機能のキーワード: rossmann fold, glutamate dehydrogenase, oxidoreductase
• 由来する生物種: Corynebacterium glutamicum
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 316389.15

構造登録者

Tomita, T.,Nishiyama, M. (登録日: 2016-08-28, 公開日: 2017-06-07, 最終更新日: 2023-11-08)

主引用文献

Tomita, T.,Yin, L.,Nakamura, S.,Kosono, S.,Kuzuyama, T.,Nishiyama, M.
Crystal structure of the 2-iminoglutarate-bound complex of glutamate dehydrogenase from Corynebacterium glutamicum
FEBS Lett., 591:1611-1622, 2017

PubMed Abstract: The NADP -dependent glutamate dehydrogenase from Corynebacterium glutamicum (CgGDH) is considered to be one of the key enzymes in the industrial fermentation of glutamate due to its high glutamate-producing activity. We determined the crystal structure of CgGDH complexed with NADP and 2-iminoglutarate. Among six subunits of hexameric CgGDH-binding NADP , only four subunits bind 2-iminoglutarate in a closed form, while the other two are in an open form. In the closed form, 2-iminoglutarate is bound to the substrate-binding site with the 2-imino group stacked by the nicotinamide ring of the coenzyme, suggesting a prehydride transfer state in a hypothesized reaction scheme with the imino intermediate. We also conducted MD simulations and provide insights into the extreme preference for the glutamate-producing reaction of CgGDH.

PubMed: 28486765
DOI: 10.1002/1873-3468.12667

実験手法

X-RAY DIFFRACTION (1.68 Å)