Structural highlights
Function
MTMB1_METBA Catalyzes the transfer of the methyl group from monomethylamine to the corrinoid cofactor of MtmC (MtmC1 or MtmC2).[1] [2]
Publication Abstract from PubMed
Genes encoding methanogenic methylamine methyltransferases all contain an in-frame amber (UAG) codon that is read through during translation. We have identified the UAG-encoded residue in a 1.55 angstrom resolution structure of the Methanosarcina barkeri monomethylamine methyltransferase (MtmB). This structure reveals a homohexamer comprised of individual subunits with a TIM barrel fold. The electron density for the UAG-encoded residue is distinct from any of the 21 natural amino acids. Instead it appears consistent with a lysine in amide-linkage to (4R,5R)-4-substituted-pyrroline-5-carboxylate. We suggest that this amino acid be named l-pyrrolysine.
A new UAG-encoded residue in the structure of a methanogen methyltransferase.,Hao B, Gong W, Ferguson TK, James CM, Krzycki JA, Chan MK Science. 2002 May 24;296(5572):1462-6. PMID:12029132[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Burke SA, Lo SL, Krzycki JA. Clustered genes encoding the methyltransferases of methanogenesis from monomethylamine. J Bacteriol. 1998 Jul;180(13):3432-40. PMID:9642198
- ↑ Burke SA, Krzycki JA. Reconstitution of Monomethylamine:Coenzyme M methyl transfer with a corrinoid protein and two methyltransferases purified from Methanosarcina barkeri. J Biol Chem. 1997 Jun 27;272(26):16570-7. PMID:9195968
- ↑ Hao B, Gong W, Ferguson TK, James CM, Krzycki JA, Chan MK. A new UAG-encoded residue in the structure of a methanogen methyltransferase. Science. 2002 May 24;296(5572):1462-6. PMID:12029132 doi:10.1126/science.1069556
