7F4C

The crystal structure of the immature holo-enzyme of homoserine dehydrogenase complexed with NADP and 1,4-butandiol from the hyperthermophilic archaeon Sulfurisphaera tokodaii.

7F4C の概要

• エントリーDOI: 10.2210/pdb7f4c/pdb
• 関連するPDBエントリー: 7F4B
• 分子名称: Homoserine dehydrogenase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, 1,4-BUTANEDIOL, ... (4 entities in total)
• 機能のキーワード: heat-induced activation, oxidoreductase
• 由来する生物種: Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) (Sulfolobus tokodaii)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 68490.04

構造登録者

Ogata, K.,Kaneko, R.,Kubota, T.,Watanabe, K.,Kurihara, E.,Oshima, T.,Yoshimune, K.,Goto, M. (登録日: 2021-06-18, 公開日: 2022-06-22, 最終更新日: 2024-10-16)

主引用文献

Kubota, T.,Kurihara, E.,Watanabe, K.,Ogata, K.,Kaneko, R.,Goto, M.,Ohshima, T.,Yoshimune, K.
Conformational changes in the catalytic region are responsible for heat-induced activation of hyperthermophilic homoserine dehydrogenase.
Commun Biol, 5:704-704, 2022

PubMed Abstract: When overexpressed as an immature enzyme in the mesophilic bacterium Escherichia coli, recombinant homoserine dehydrogenase from the hyperthermophilic archaeon Sulfurisphaera tokodaii (StHSD) was markedly activated by heat treatment. Both the apo- and holo-forms of the immature enzyme were successively crystallized, and the two structures were determined. Comparison among the structures of the immature enzyme and previously reported structures of mature enzymes revealed that a conformational change in a flexible part (residues 160-190) of the enzyme, which encloses substrates within the substrate-binding pocket, is smaller in the immature enzyme. The immature enzyme, but not the mature enzyme, formed a complex that included NADP, despite its absence during crystallization. This indicates that the opening to the substrate-binding pocket in the immature enzyme is not sufficient for substrate-binding, efficient catalytic turnover or release of NADP. Thus, specific conformational changes within the catalytic region appear to be responsible for heat-induced activation.

PubMed: 35835834
DOI: 10.1038/s42003-022-03656-7

実験手法

X-RAY DIFFRACTION (1.9 Å)