3POT

Structural analysis of a Ni(III)-methyl species in methyl-coenzyme M reductase from Methanothermobacter marburgensis

Summary for 3POT

• Entry DOI: 10.2210/pdb3pot/pdb
• Descriptor: Methyl-coenzyme M reductase I subunit alpha, POTASSIUM ION, 1,2-ETHANEDIOL, ... (12 entities in total)
• Functional Keywords: metal-binding, nickel, methyl-coenzyme m reductase, methanogenesis, methylation, transferase
• Biological source: Methanothermobacter marburgensis (Methanobacterium thermoautotrophicum); More
• Total number of polymer chains: 6
• Total formula weight: 277552.69

Authors

Cedervall, P.E.,Wilmot, C.M. (deposition date: 2010-11-23, release date: 2011-04-13, Last modification date: 2023-09-06)

Primary citation

Cedervall, P.E.,Dey, M.,Li, X.,Sarangi, R.,Hedman, B.,Ragsdale, S.W.,Wilmot, C.M.
Structural Analysis of a Ni-Methyl Species in Methyl-Coenzyme M Reductase from Methanothermobacter marburgensis.
J.Am.Chem.Soc., 133:5626-5628, 2011

PubMed Abstract: We present the 1.2 Å resolution X-ray crystal structure of a Ni-methyl species that is a proposed catalytic intermediate in methyl-coenzyme M reductase (MCR), the enzyme that catalyzes the biological formation of methane. The methyl group is situated 2.1 Å proximal of the Ni atom of the MCR coenzyme F(430). A rearrangement of the substrate channel has been posited to bring together substrate species, but Ni(III)-methyl formation alone does not lead to any observable structural changes in the channel.

PubMed: 21438550
DOI: 10.1021/ja110492p

Experimental method

X-RAY DIFFRACTION (1.2 Å)