8W33

Structure of McrD (methyl-coenzyme M reductase operon protein D) from Methanomassiliicoccus luminyensis

8W33 の概要

• エントリーDOI: 10.2210/pdb8w33/pdb
• 分子名称: McrD (methyl-coenzyme M reductase operon protein D), GLYCEROL (3 entities in total)
• 機能のキーワード: methyl-coenzyme m reductase-associated, methanogenesis, ferredoxin-like, alpha/beta barrel, unknown function
• 由来する生物種: Methanomassiliicoccus luminyensis B10
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 39038.75

構造登録者

Sutherland-Smith, A.J.,Carbone, V.,Schofield, L.R.,Ronimus, R.S. (登録日: 2024-02-21, 公開日: 2024-07-03, 最終更新日: 2024-08-28)

主引用文献

Sutherland-Smith, A.J.,Carbone, V.,Schofield, L.R.,Cronin, B.,Duin, E.C.,Ronimus, R.S.
The crystal structure of methanogen McrD, a methyl-coenzyme M reductase-associated protein.
Febs Open Bio, 14:1222-1229, 2024

PubMed Abstract: Methyl-coenzyme M reductase (MCR) is a multi-subunit (αβγ) enzyme responsible for methane formation via its unique F cofactor. The genes responsible for producing MCR (mcrA, mcrB and mcrG) are typically colocated with two other highly conserved genes mcrC and mcrD. We present here the high-resolution crystal structure for McrD from a human gut methanogen Methanomassiliicoccus luminyensis strain B10. The structure reveals that McrD comprises a ferredoxin-like domain assembled into an α + β barrel-like dimer with conformational flexibility exhibited by a functional loop. The description of the M. luminyensis McrD crystal structure contributes to our understanding of this key conserved methanogen protein typically responsible for promoting MCR activity and the production of methane, a greenhouse gas.

PubMed: 38877345
DOI: 10.1002/2211-5463.13848

実験手法

X-RAY DIFFRACTION (1.65 Å)