1mro

METHYL-COENZYME M REDUCTASE

spinqualitylabelsall models 1mro, resolution 1.16Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1mro is a 6 chain structure with sequence from Methanothermobacter marburgensis str. Marburg. The November 2014 RCSB PDB Molecule of the Month feature on Methyl-coenzyme M Reductase by David Goodsell is 10.2210/rcsb_pdb/mom_2014_11. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.16Å Ligands: AGM, COM, GL3, GOL, MGN, MHS, NA, SMC, TP7, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MCRA_METTM Reduction of methyl-coenzyme M (2-(methylthio) ethanesulfonic acid) with 7-mercaptoheptanoylthreonine phosphate to methane and a heterodisulfide. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Methyl-coenzyme M reductase (MCR), the enzyme responsible for the microbial formation of methane, is a 300-kilodalton protein organized as a hexamer in an alpha2beta2gamma2 arrangement. The crystal structure of the enzyme from Methanobacterium thermoautotrophicum, determined at 1.45 angstrom resolution for the inactive enzyme state MCRox1-silent, reveals that two molecules of the nickel porphinoid coenzyme F430 are embedded between the subunits alpha, alpha', beta, and gamma and alpha', alpha, beta', and gamma', forming two identical active sites. Each site is accessible for the substrate methyl-coenzyme M through a narrow channel locked after binding of the second substrate coenzyme B. Together with a second structurally characterized enzyme state (MCRsilent) containing the heterodisulfide of coenzymes M and B, a reaction mechanism is proposed that uses a radical intermediate and a nickel organic compound. Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation.,Ermler U, Grabarse W, Shima S, Goubeaud M, Thauer RK Science. 1997 Nov 21;278(5342):1457-62. PMID:9367957 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA