3ASU

Crystal structure of serine dehydrogenase from Escherichia coli

3ASU の概要

• エントリーDOI: 10.2210/pdb3asu/pdb
• 関連するPDBエントリー: 3ASV
• 分子名称: Short-chain dehydrogenase/reductase SDR (2 entities in total)
• 機能のキーワード: sdr family, rossmann-fold, short-chain dehydrogenase/reductase, l-allo-threonine dehydrogenase, oxidoreductase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 54555.77

構造登録者

Yamazawa, R.,Nakajima, Y.,Yoshimoto, T.,Ito, K. (登録日: 2010-12-21, 公開日: 2011-10-12, 最終更新日: 2023-11-01)

主引用文献

Yamazawa, R.,Nakajima, Y.,Mushiake, K.,Yoshimoto, T.,Ito, K.
Crystal structure of serine dehydrogenase from Escherichia coli: important role of the C-terminal region for closed-complex formation.
J.Biochem., 149:701-712, 2011

PubMed Abstract: Serine dehydrogenase from Escherichia coli is a homotetrameric enzyme belonging to the short-chain dehydrogenase/reductase (SDR) family. This enzyme catalyses the NADP(+)-dependent oxidation of serine to 2-aminomalonate semialdehyde. The enzyme shows a stereospecificity for β-(3S)-hydroxy acid as a substrate; however, no stereospecificity was observed at the α-carbon. The structures of the ligand-free SerDH and SerDH-NADP(+)-phosphate complex were determined at 1.9 and 2.7 Å resolutions, respectively. The overall structure, including the catalytic tetrad of Asn106, Ser134, Tyr147 and Lys151, shows obvious relationships with other members of the SDR family. The structure of the substrate-binding loop and that of the C-terminal region were disordered in the ligand-free enzyme, whereas these structures were clearly defined in the SerDH-NADP(+) complex as a closed form. Interestingly, the C-terminal region was protruded from the main body and it formed an anti-parallel β-sheet with another C-terminal region on the subunit that is diagonally opposite to that in the tetramer. It is revealed that the C-terminal region possesses the important roles in substrate binding through the stabilization of the substrate-binding loop in the closed form complex. The roles of the C-terminal region along with those of the residues involved in substrate recognition were studied by site-directed mutagenesis.

PubMed: 21349860
DOI: 10.1093/jb/mvr024

実験手法

X-RAY DIFFRACTION (1.9 Å)