4XB1

Hyperthermophilic archaeal homoserine dehydrogenase in complex with NADPH

4XB1 の概要

• エントリーDOI: 10.2210/pdb4xb1/pdb
• 関連するPDBエントリー: 4XB2
• 分子名称: 319aa long hypothetical homoserine dehydrogenase, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, SODIUM ION, ... (5 entities in total)
• 機能のキーワード: rossmann fold, oxidoreductase
• 由来する生物種: Pyrococcus horikoshii OT3
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 76077.68

構造登録者

Sakuraba, H.,Inoue, S.,Yoneda, K.,Ohshima, T. (登録日: 2014-12-16, 公開日: 2015-07-15, 最終更新日: 2023-11-08)

主引用文献

Hayashi, J.,Inoue, S.,Kim, K.,Yoneda, K.,Kawarabayasi, Y.,Ohshima, T.,Sakuraba, H.
Crystal Structures of a Hyperthermophilic Archaeal Homoserine Dehydrogenase Suggest a Novel Cofactor Binding Mode for Oxidoreductases.
Sci Rep, 5:11674-11674, 2015

PubMed Abstract: NAD(P)-dependent dehydrogenases differ according to their coenzyme preference: some prefer NAD, others NADP, and still others exhibit dual cofactor specificity. The structure of a newly identified archaeal homoserine dehydrogenase showed this enzyme to have a strong preference for NADP. However, NADP did not act as a cofactor with this enzyme, but as a strong inhibitor of NAD-dependent homoserine oxidation. Structural analysis and site-directed mutagenesis showed that the large number of interactions between the cofactor and the enzyme are responsible for the lack of reactivity of the enzyme towards NADP. This observation suggests this enzyme exhibits a new variation on cofactor binding to a dehydrogenase: very strong NADP binding that acts as an obstacle to NAD(P)-dependent dehydrogenase catalytic activity.

PubMed: 26154028
DOI: 10.1038/srep11674

実験手法

X-RAY DIFFRACTION (2.3 Å)