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

被引:315
作者
Hao, B
Gong, WM
Ferguson, TK
James, CM
Krzycki, JA
Chan, MK
机构
[1] Ohio State Univ, Dept Biochem, Columbus, OH 43210 USA
[2] Ohio State Univ, Dept Chem, Columbus, OH 43210 USA
[3] Ohio State Univ, Dept Microbiol, Columbus, OH 43210 USA
关键词
D O I
10.1126/science.1069556
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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,SR)-4-substituted-pyrroline-5-carboxylate. We suggest that this amino acid be named L-pyrrolysine.
引用
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页码:1462 / 1466
页数:5
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