3HRD

Crystal structure of nicotinate dehydrogenase

3HRD の概要

• エントリーDOI: 10.2210/pdb3hrd/pdb
• 分子名称: Nicotinate dehydrogenase large molybdopterin subunit, NICOTINIC ACID, FLAVIN-ADENINE DINUCLEOTIDE, ... (14 entities in total)
• 機能のキーワード: selenium ligand, 2fe-2s, iron, iron-sulfur, metal-binding, oxidoreductase
• 由来する生物種: Eubacterium barkeri (Clostridium barkeri); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 266092.39

構造登録者

Wagener, N.,Pierik, A.J.,Hille, R.,Dobbek, H. (登録日: 2009-06-09, 公開日: 2009-06-30, 最終更新日: 2023-11-01)

主引用文献

Wagener, N.,Pierik, A.J.,Ibdah, A.,Hille, R.,Dobbek, H.
The Mo-Se active site of nicotinate dehydrogenase
Proc.Natl.Acad.Sci.USA, 106:11055-11060, 2009

PubMed Abstract: Nicotinate dehydrogenase (NDH) from Eubacterium barkeri is a molybdoenzyme catalyzing the hydroxylation of nicotinate to 6-hydroxynicotinate. Reactivity of NDH critically depends on the presence of labile (nonselenocysteine) selenium with an as-yet-unidentified form and function. We have determined the crystal structure of NDH and analyzed its active site by multiple wavelengths anomalous dispersion methods. We show that selenium is bound as a terminal Mo=Se ligand to molybdenum and that it occupies the position of the terminal sulfido ligand in other molybdenum hydroxylases. The role of selenium in catalysis has been assessed by model calculations, which indicate an acceleration of the critical hydride transfer from the substrate to the selenido ligand in the course of substrate hydroxylation when compared with an active site containing a sulfido ligand. The MoO(OH)Se active site of NDH shows a novel type of utilization and reactivity of selenium in nature.

PubMed: 19549881
DOI: 10.1073/pnas.0902210106

実験手法

X-RAY DIFFRACTION (2.2 Å)