6TGA

Cryo-EM Structure of as isolated form of NAD+-dependent Formate Dehydrogenase from Rhodobacter capsulatus

6TGA の概要

• エントリーDOI: 10.2210/pdb6tga/pdb
• EMDBエントリー: 10496
• 分子名称: Formate dehydrogenase subunit alpha, FLAVIN MONONUCLEOTIDE, Formate dehydrogenase subunit beta, ... (10 entities in total)
• 機能のキーワード: molybdoenzyme, formate oxidation, nad+-dependent, oxidoreductase
• 由来する生物種: Rhodobacter capsulatus; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 369027.76

構造登録者

Wendler, P.,Radon, C.,Mittelstaedt, G. (登録日: 2019-11-15, 公開日: 2020-04-22, 最終更新日: 2024-05-22)

主引用文献

Radon, C.,Mittelstadt, G.,Duffus, B.R.,Burger, J.,Hartmann, T.,Mielke, T.,Teutloff, C.,Leimkuhler, S.,Wendler, P.
Cryo-EM structures reveal intricate Fe-S cluster arrangement and charging in Rhodobacter capsulatus formate dehydrogenase.
Nat Commun, 11:1912-1912, 2020

PubMed Abstract: Metal-containing formate dehydrogenases (FDH) catalyse the reversible oxidation of formate to carbon dioxide at their molybdenum or tungsten active site. They display a diverse subunit and cofactor composition, but structural information on these enzymes is limited. Here we report the cryo-electron microscopic structures of the soluble Rhodobacter capsulatus FDH (RcFDH) as isolated and in the presence of reduced nicotinamide adenine dinucleotide (NADH). RcFDH assembles into a 360 kDa dimer of heterotetramers revealing a putative interconnection of electron pathway chains. In the presence of NADH, the RcFDH structure shows charging of cofactors, indicative of an increased electron load.

PubMed: 32313256
DOI: 10.1038/s41467-020-15614-0

実験手法

ELECTRON MICROSCOPY (3.26 Å)