8W33

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

Summary for 8W33

• Entry DOI: 10.2210/pdb8w33/pdb
• Descriptor: McrD (methyl-coenzyme M reductase operon protein D), GLYCEROL (3 entities in total)
• Functional Keywords: methyl-coenzyme m reductase-associated, methanogenesis, ferredoxin-like, alpha/beta barrel, unknown function
• Biological source: Methanomassiliicoccus luminyensis B10
• Total number of polymer chains: 2
• Total formula weight: 39038.75

Authors

Sutherland-Smith, A.J.,Carbone, V.,Schofield, L.R.,Ronimus, R.S. (deposition date: 2024-02-21, release date: 2024-07-03, Last modification date: 2024-08-28)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.65 Å)