8gf5

From Proteopedia

McrD binds asymmetrically to methyl-coenzyme M reductase improving active site accessibility during assembly

Structural highlights

8gf5 is a 7 chain structure with sequence from Methanosarcina acetivorans C2A. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 3Å
Ligands:	, , , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MCRA_METAC Component of the methyl-coenzyme M reductase (MCR) I that catalyzes the reductive cleavage of methyl-coenzyme M (CoM-S-CH3 or 2-(methylthio)ethanesulfonate) using coenzyme B (CoB or 7-mercaptoheptanoylthreonine phosphate) as reductant which results in the production of methane and the mixed heterodisulfide of CoB and CoM (CoM-S-S-CoB). This is the final step in methanogenesis.[UniProtKB:P11558]

Publication Abstract from PubMed

Methyl-coenzyme M reductase (MCR) catalyzes the formation of methane, and its activity accounts for nearly all biologically produced methane released into the atmosphere. The assembly of MCR is an intricate process involving the installation of a complex set of posttranslational modifications and the unique Ni-containing tetrapyrrole called coenzyme F(430). Despite decades of research, details of MCR assembly remain largely unresolved. Here, we report the structural characterization of MCR in two intermediate states of assembly. These intermediate states lack one or both F(430) cofactors and form complexes with the previously uncharacterized McrD protein. McrD is found to bind asymmetrically to MCR, displacing large regions of the alpha subunit and increasing active-site accessibility for the installation of F(430)-shedding light on the assembly of MCR and the role of McrD therein. This work offers crucial information for the expression of MCR in a heterologous host and provides targets for the design of MCR inhibitors.

McrD binds asymmetrically to methyl-coenzyme M reductase improving active-site accessibility during assembly.,Chadwick GL, Joiner AMN, Ramesh S, Mitchell DA, Nayak DD Proc Natl Acad Sci U S A. 2023 Jun 20;120(25):e2302815120. doi: , 10.1073/pnas.2302815120. Epub 2023 Jun 12. PMID:37307484^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Chadwick GL, Joiner AMN, Ramesh S, Mitchell DA, Nayak DD. McrD binds asymmetrically to methyl-coenzyme M reductase improving active-site accessibility during assembly. Proc Natl Acad Sci U S A. 2023 Jun 20;120(25):e2302815120. PMID:37307484 doi:10.1073/pnas.2302815120