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1L2Q

Crystal Structure of the Methanosarcina barkeri Monomethylamine Methyltransferase (MtmB)

Summary for 1L2Q
Entry DOI10.2210/pdb1l2q/pdb
Related1L2R
Descriptormonomethylamine methyltransferase, AMMONIUM ION (3 entities in total)
Functional Keywordstim barrel, transferase
Biological sourceMethanosarcina barkeri
Total number of polymer chains1
Total formula weight50326.30
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 citationHao, 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: 12029132
DOI: 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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