5GLG

The novel function of Osm1 under anaerobic condition in the ER was revealed by crystal structure of Osm1, a soluble fumarate reductase in yeast

5GLG の概要

• エントリーDOI: 10.2210/pdb5glg/pdb
• 分子名称: Fumarate reductase 2, SUCCINIC ACID, FLAVIN-ADENINE DINUCLEOTIDE, ... (4 entities in total)
• 機能のキーワード: osm1, fumarate reductase, fad, oxidoreductase
• 由来する生物種: Saccharomyces cerevisiae S288c (Baker's yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 52499.31

構造登録者

Park, H.H.,Choi, J.Y. (登録日: 2016-07-11, 公開日: 2017-07-12, 最終更新日: 2024-03-20)

主引用文献

Kim, S.,Kim, C.M.,Son, Y.J.,Choi, J.Y.,Siegenthaler, R.K.,Lee, Y.,Jang, T.H.,Song, J.,Kang, H.,Kaiser, C.A.,Park, H.H.
Molecular basis of maintaining an oxidizing environment under anaerobiosis by soluble fumarate reductase.
Nat Commun, 9:4867-4867, 2018

PubMed Abstract: Osm1 and Frd1 are soluble fumarate reductases from yeast that are critical for allowing survival under anaerobic conditions. Although they maintain redox balance during anaerobiosis, the underlying mechanism is not understood. Here, we report the crystal structure of a eukaryotic soluble fumarate reductase, which is unique among soluble fumarate reductases as it lacks a heme domain. Structural and enzymatic analyses indicate that Osm1 has a specific binding pocket for flavin molecules, including FAD, FMN, and riboflavin, catalyzing their oxidation while reducing fumarate to succinate. Moreover, ER-resident Osm1 can transfer electrons from the Ero1 FAD cofactor to fumarate either by free FAD or by a direct interaction, allowing de novo disulfide bond formation in the absence of oxygen. We conclude that soluble eukaryotic fumarate reductases can maintain an oxidizing environment under anaerobic conditions, either by oxidizing cellular flavin cofactors or by a direct interaction with flavoenzymes such as Ero1.

PubMed: 30451826
DOI: 10.1038/s41467-018-07285-9

実験手法

X-RAY DIFFRACTION (1.8 Å)