1nth

Crystal structure of the methanosarcina barkeri monomethylamine methyltransferase (MTMB)

spinqualitylabelsall models 1nth, resolution 1.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1nth is a 1 chain structure with sequence from Methanosarcina barkeri. This structure supersedes the now removed PDB entry 1l2r. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1l2q Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [MTMB1_METBA] Catalyzes the transfer of the methyl group from monomethylamine to the corrinoid cofactor of MtmC (MtmC1 or MtmC2). 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Pyrrolysine

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