8RR0

CryoEM structure of Molybdenum bispyranopterin guanine dinucleotide formate dehydrogenases ForCE1 from Bacillus subtilis

これはPDB形式変換不可エントリーです。

8RR0 の概要

• エントリーDOI: 10.2210/pdb8rr0/pdb
• EMDBエントリー: 19452
• 分子名称: Uncharacterized protein YjgD, 2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE GUANOSINE DINUCLEOTIDE, MOLYBDENUM(IV) ION, ... (14 entities in total)
• 機能のキーワード: bacterial metabolism bioenergetics metalloenzyme quinone iron-sulfur cluster helical membrane plug-in, oxidoreductase
• 由来する生物種: Bacillus subtilis subsp. subtilis str. 168; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 556373.74

構造登録者

Cherrier, M.V.,Arnoux, P.,Martin, L.,Nicolet, Y.,Schoehn, G.,Legrand, P.,Broc, M.,Seduk, F.,Brasseur, G.,Arias-Cartin, R.,Magalon, A.,Walburger, A.,Uzel, A.,Guigliarelli, B.,Grimaldi, S.,Pierrel, F.,Mate, M. (登録日: 2024-01-22, 公開日: 2025-08-06, 最終更新日: 2025-11-26)

主引用文献

Broc, M.,Cherrier, M.V.,Uzel, A.,Arias-Cartin, R.,Arnoux, P.,Brasseur, G.,Seduk, F.,Guigliarelli, B.,Legrand, P.,Pierrel, F.,Schoehn, G.,Mate, M.J.,Martin, L.,Grimaldi, S.,Nicolet, Y.,Magalon, A.,Walburger, A.
A scaffold for quinone channeling between membrane and soluble bacterial oxidoreductases.
Nat.Struct.Mol.Biol., 32:2196-2202, 2025

PubMed Abstract: Redox processes are at the heart of energetic metabolism that drives life on earth. By extension, complex and efficient electron transfer wires are necessary to connect the various metabolic pathways that are often located in distinct cellular compartments. Here, we uncovered a structural module that enables channeling of quinones from the membrane to various water-soluble redox catalytic units in prokaryotes. Using X-ray crystallography and cryo-electron microscopy, we determined the structure of the unusual bacterial formate dehydrogenase ForCE that contains four ForC catalytic subunits docked around a membrane-associated tetrameric ForE central scaffold. In the latter, a conserved domain that we propose to name helical membrane plugin (HMP) was identified as essential to link formate oxidation, in Bacillus subtilis, to the aerobic respiratory chain. Our bioinformatic analysis indicates that this HMP is associated with different quinone-reducing oxidoreductases, highlighting its broad importance as a functional unit to wire electrons between a given catalytic redox center and the quinone pool.

PubMed: 40855134
DOI: 10.1038/s41594-025-01607-4

実験手法

ELECTRON MICROSCOPY (3.35 Å)