4LSW

Crystallization and Structural Analysis of 2-Hydroxyacid Dehydrogenase from Ketogulonicigenium vulgare Y25

4LSW の概要

• エントリーDOI: 10.2210/pdb4lsw/pdb
• 分子名称: D-2-hydroxyacid dehydrogensase protein (2 entities in total)
• 機能のキーワード: hydrogenase, hydrolase
• 由来する生物種: Ketogulonicigenium vulgare
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34394.13

構造登録者

Han, X.,Liu, X. (登録日: 2013-07-23, 公開日: 2013-09-11, 最終更新日: 2023-11-08)

主引用文献

Han, X.,Xiong, X.,Hu, X.,Li, M.,Zhang, W.,Liu, X.
Crystallization and structural analysis of 2-hydroxyacid dehydrogenase from Ketogulonicigenium vulgare.
Biotechnol.Lett., 36:295-300, 2014

PubMed Abstract: L-2-Hydroxyacid dehydrogenase (HDH) from Ketogulonicigenium vulgare Y25 was cloned and overexpressed in Escherichia coli. The protein was purified and crystallized by the sitting-drop vapour-diffusion method with polyethylene glycol 3350 as precipitant. The crystal structure of HDH was determined at 1.64 Å resolution using the molecular replacement method with the crystal structure of hydroxyl (phenyl) pyruvate reductase from Coleus blumei Benth as the search model. The overall structure of HDH was similar to that of hydroxyl(phenyl)pyruvate reductase, consisting of two compact domains separated by a deep active cleft. The most significant structural divergence is located around the pocket gate comprising residues A210, T211 and R212, which is located on top of the catalytic triad.

PubMed: 24068509
DOI: 10.1007/s10529-013-1354-8

実験手法

X-RAY DIFFRACTION (1.64 Å)