1l2q
Crystal Structure of the Methanosarcina barkeri Monomethylamine Methyltransferase (MtmB)Crystal Structure of the Methanosarcina barkeri Monomethylamine Methyltransferase (MtmB)
Structural highlights
FunctionMTMB1_METBA Catalyzes the transfer of the methyl group from monomethylamine to the corrinoid cofactor of MtmC (MtmC1 or MtmC2).[1] [2] Publication Abstract from PubMedGenes 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 AlsoReferences
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