Structural highlights
Publication Abstract from PubMed
Methyl-coenzyme M reductase (MCR) is a multi-subunit (alpha(2)beta(2)gamma(2)) enzyme responsible for methane formation via its unique F(430) 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 alpha + beta 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.
The crystal structure of methanogen McrD, a methyl-coenzyme M reductase-associated protein.,Sutherland-Smith AJ, Carbone V, Schofield LR, Cronin B, Duin EC, Ronimus RS FEBS Open Bio. 2024 Jun 14. doi: 10.1002/2211-5463.13848. PMID:38877345[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sutherland-Smith AJ, Carbone V, Schofield LR, Cronin B, Duin EC, Ronimus RS. The crystal structure of methanogen McrD, a methyl-coenzyme M reductase-associated protein. FEBS Open Bio. 2024 Jun 14. PMID:38877345 doi:10.1002/2211-5463.13848
