4E5M

Thermostable phosphite dehydrogenase E175A/A176R in complex with NADP

4E5M の概要

• エントリーDOI: 10.2210/pdb4e5m/pdb
• 関連するPDBエントリー: 4E5K 4E5N 4E5P
• 分子名称: Thermostable phosphite dehydrogenase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total)
• 機能のキーワード: d-2-hydroxyacid dehydrogenase, oxidoreductase
• 由来する生物種: Pseudomonas stutzeri
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 73363.54

構造登録者

Zou, Y.,Zhang, H.,Nair, S.K. (登録日: 2012-03-14, 公開日: 2012-05-30, 最終更新日: 2024-04-03)

主引用文献

Zou, Y.,Zhang, H.,Brunzelle, J.S.,Johannes, T.W.,Woodyer, R.,Hung, J.E.,Nair, N.,van der Donk, W.A.,Zhao, H.,Nair, S.K.
Crystal structures of phosphite dehydrogenase provide insights into nicotinamide cofactor regeneration.
Biochemistry, 51:4263-4270, 2012

PubMed Abstract: The enzyme phosphite dehydrogenase (PTDH) catalyzes the NAD(+)-dependent conversion of phosphite to phosphate and represents the first biological catalyst that has been shown to conduct the enzymatic oxidation of phosphorus. Despite investigation for more than a decade into both the mechanism of its unusual reaction and its utility in cofactor regeneration, there has been a lack of any structural data for PTDH. Here we present the cocrystal structure of an engineered thermostable variant of PTDH bound to NAD(+) (1.7 Å resolution), as well as four other cocrystal structures of thermostable PTDH and its variants with different ligands (all between 1.85 and 2.3 Å resolution). These structures provide a molecular framework for understanding prior mutational analysis and point to additional residues, located in the active site, that may contribute to the enzymatic activity of this highly unusual catalyst.

PubMed: 22564171
DOI: 10.1021/bi2016926

実験手法

X-RAY DIFFRACTION (1.85 Å)