8w33 | pdb_00008w33

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

spinqualitylabelsall models 8w33, resolution 1.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8w33 is a 2 chain structure with sequence from Methanomassiliicoccus luminyensis B10. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.65Å Ligands: GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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