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A New UAG-Encoded Residue in the Structure of a Methanogen Methyltransferase

Science  24 May 2002:
Vol. 296, Issue 5572, pp. 1462-1466
DOI: 10.1126/science.1069556

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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 barkerimonomethylamine 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.

  • * To whom correspondence should be addressed: E-mail: chan{at}chemistry.ohio-state.edu and krzycki.1{at}osu.edu

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