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Science. 2002 May 24;296(5572):1462-6.

A new UAG-encoded residue in the structure of a methanogen methyltransferase.

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  • 1Department of Biochemistry, The Ohio State University, 484 West 12th Avenue, Columbus, OH 43210, USA.

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.

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PMID:
12029132
[PubMed - indexed for MEDLINE]
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