1L2Q
Crystal Structure of the Methanosarcina barkeri Monomethylamine Methyltransferase (MtmB)
Summary for 1L2Q
Entry DOI | 10.2210/pdb1l2q/pdb |
Related | 1L2R |
Descriptor | monomethylamine methyltransferase, AMMONIUM ION (3 entities in total) |
Functional Keywords | tim barrel, transferase |
Biological source | Methanosarcina barkeri |
Total number of polymer chains | 1 |
Total formula weight | 50326.30 |
Authors | Hao, B.,Gong, W.,Ferguson, T.K.,James, C.M.,Krzycki, J.A.,Chan, M.K. (deposition date: 2002-02-24, release date: 2002-06-05, Last modification date: 2025-03-26) |
Primary citation | Hao, B.,Gong, W.,Ferguson, T.K.,James, C.M.,Krzycki, J.A.,Chan, M.K. A new UAG-encoded residue in the structure of a methanogen methyltransferase. Science, 296:1462-1466, 2002 Cited by PubMed Abstract: 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. PubMed: 12029132DOI: 10.1126/science.1069556 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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