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Science 24 May 2002:
Vol. 296. no. 5572, pp. 1462 - 1466
DOI: 10.1126/science.1069556
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Reports

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

Bing Hao,1 Weimin Gong,1 Tsuneo K. Ferguson,2 Carey M. James,2 Joseph A. Krzycki,2* Michael K. Chan1*

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.

1 Departments of Biochemistry and Chemistry, and
2 Department of Microbiology, The Ohio State University, 484 West 12th Avenue, Columbus, OH 43210, USA.
*   To whom correspondence should be addressed: E-mail: chan{at}chemistry.ohio-state.edu and krzycki.1{at}osu.edu

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