6BKA

Crystal Structure of Nitronate Monooxygenase from Cyberlindnera saturnus

6BKA の概要

• エントリーDOI: 10.2210/pdb6bka/pdb
• 分子名称: Nitronate monooxygenase, FLAVIN MONONUCLEOTIDE, 3,6,9,12,15,18,21,24,27,30,33,36-dodecaoxaoctatriacontane-1,38-diol, ... (5 entities in total)
• 機能のキーワード: monooxygenase, propionate 3-nitronate, oxidoreductase
• 由来する生物種: Cyberlindnera mrakii (Yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 42685.12

構造登録者

Agniswamy, J.,Fang, Y.-F.,Weber, I.T. (登録日: 2017-11-08, 公開日: 2018-02-14, 最終更新日: 2024-11-06)

主引用文献

Agniswamy, J.,Reis, R.A.G.,Wang, Y.F.,Smitherman, C.,Su, D.,Weber, I.,Gadda, G.
Crystal structure of yeast nitronate monooxygenase from Cyberlindnera saturnus.
Proteins, 86:599-605, 2018

PubMed Abstract: Nitronate monooxygenase (NMO) is an FMN-dependent enzyme that oxidizes the neurotoxin propionate 3-nitronate (P3N) and represents the best-known system for P3N detoxification in different organisms. The crystal structure of the first eukaryotic Class I NMO from Cyberlindnera saturnus (CsNMO) has been solved at 1.65 Å resolution and refined to an R-factor of 14.0%. The three-dimensional structures of yeast CsNMO and bacterial PaNMO are highly conserved with the exception of three additional loops on the surface in the CsNMO enzyme and differences in four active sites residues. A PEG molecule was identified in the structure and formed extensive interactions with CsNMO, suggesting a specific binding site; however, 8% PEG showed no significant effect on the enzyme activity. This new crystal structure of a eukaryotic NMO provides insight into the function of this class of enzymes.

PubMed: 29383742
DOI: 10.1002/prot.25470

実験手法

X-RAY DIFFRACTION (1.65 Å)