Structural highlights
7qbs is a 2 chain structure with sequence from Methanosarcina acetivorans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Method: | X-ray diffraction, Resolution 2.327Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
MCRAM_METAC Radical SAM methyltransferase that is responsible for the C(5)-methylation of 'Arg-285' of the methyl-coenzyme M reductase (MCR) subunit alpha McrA. This post-translational methylation, despite being not essential in vivo, plays a role for the stability and structural integrity of MCR.[1]
Publication Abstract from PubMed
By catalysing the microbial formation of methane, methyl-coenzyme M reductase has a central role in the global levels of this greenhouse gas(1,2). The activity of methyl-coenzyme M reductase is profoundly affected by several unique post-translational modifications(3-6), such as a unique C-methylation reaction catalysed by methanogenesis marker protein 10 (Mmp10), a radical S-adenosyl-L-methionine (SAM) enzyme(7,8). Here we report the spectroscopic investigation and atomic resolution structure of Mmp10 from Methanosarcina acetivorans, a unique B12 (cobalamin)-dependent radical SAM enzyme(9). The structure of Mmp10 reveals a unique enzyme architecture with four metallic centres and critical structural features involved in the control of catalysis. In addition, the structure of the enzyme-substrate complex offers a glimpse into a B12-dependent radical SAM enzyme in a precatalytic state. By combining electron paramagnetic resonance spectroscopy, structural biology and biochemistry, our study illuminates the mechanism by which the emerging superfamily of B12-dependent radical SAM enzymes catalyse chemically challenging alkylation reactions and identifies distinctive active site rearrangements to provide a structural rationale for the dual use of the SAM cofactor for radical and nucleophilic chemistry.
Crystallographic snapshots of a B12-dependent radical SAM methyltransferase.,Fyfe CD, Bernardo-Garcia N, Fradale L, Grimaldi S, Guillot A, Brewee C, Chavas LMG, Legrand P, Benjdia A, Berteau O Nature. 2022 Feb;602(7896):336-342. doi: 10.1038/s41586-021-04355-9. Epub 2022, Feb 2. PMID:35110733[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Deobald D, Adrian L, Schöne C, Rother M, Layer G. Identification of a unique Radical SAM methyltransferase required for the sp(3)-C-methylation of an arginine residue of methyl-coenzyme M reductase. Sci Rep. 2018 May 9;8(1):7404. PMID:29743535 doi:10.1038/s41598-018-25716-x
- ↑ Fyfe CD, Bernardo-Garcia N, Fradale L, Grimaldi S, Guillot A, Brewee C, Chavas LMG, Legrand P, Benjdia A, Berteau O. Crystallographic snapshots of a B12-dependent radical SAM methyltransferase. Nature. 2022 Feb;602(7896):336-342. doi: 10.1038/s41586-021-04355-9. Epub 2022, Feb 2. PMID:35110733 doi:http://dx.doi.org/10.1038/s41586-021-04355-9
