1TV3
Crystal structure of the N-methyl-hydroxylamine MtmB complex
Summary for 1TV3
| Entry DOI | 10.2210/pdb1tv3/pdb |
| Related | 1L2Q 1NTH |
| Descriptor | Monomethylamine methyltransferase mtmB1, 5-(HYDROXY-METHYL-AMINO)-3-METHYL-PYRROLIDINE-2-CARBOXYLIC ACID (3 entities in total) |
| Functional Keywords | tim barrel, transferase |
| Biological source | Methanosarcina barkeri |
| Total number of polymer chains | 1 |
| Total formula weight | 50357.31 |
| Authors | Hao, B.,Zhao, G.,Kang, P.T.,Soares, J.A.,Ferguson, T.K.,Gallucci, J.,Krzycki, J.A.,Chan, M.K. (deposition date: 2004-06-26, release date: 2004-10-19, Last modification date: 2024-10-30) |
| Primary citation | Hao, B.,Zhao, G.,Kang, P.T.,Soares, J.A.,Ferguson, T.K.,Gallucci, J.,Krzycki, J.A.,Chan, M.K. Reactivity and chemical synthesis of L-pyrrolysine- the 22(nd) genetically encoded amino acid Chem.Biol., 11:1317-1324, 2004 Cited by PubMed Abstract: L-pyrrolysine, the 22(nd) genetically encoded amino acid, was previously deduced to be (4R, 5R)-4-substituted-pyrroline-5-carboxylate attached to the epsilon-nitrogen of lysine based on the crystal structure of the M. barkeri monomethylamine methyltransferase (MtmB). To confirm L-pyrrolysine's identity, structures of MtmB have been determined following treatment with hydroxylamine, N-methylhydroxylamine, or dithionite. Analysis of these structures has provided additional support for the presence of the pyrroline ring and, together with previous mass spectroscopy data, has led us to assign the C(4)-substituent to a methyl group. Based on this assignment, synthetic L-pyrrolysine was prepared by chemical methods. Detailed study of this chemically synthesized L-pyrrolysine has allowed us to characterize its physical properties, to study its chemical stability, and to elucidate the role of its C(4) substituent. Future applications of this synthetic L-pyrrolysine include its in vivo incorporation into recombinant proteins. PubMed: 15380192DOI: 10.1016/j.chembiol.2004.07.011 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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