The DOI matches its Crossref record; 18 of the 18 references it cites were found in a registry or an index.
A New UAG-Encoded Residue in the Structure of a Methanogen Methyltransferase
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 (4 R ,5 R )-4-substituted-pyrroline-5-carboxylate. We suggest that this amino acid be named l -pyrrolysine.
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Cited by
Metabolic, Phylogenetic, and Ecological Diversity of the Methanogenic Archaea
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M ECHANISM AND R EGULATION OF S ELENOPROTEIN S YNTHESIS
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Natural expansion of the genetic code
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Metadata
- Authors
- Hao, B., Gong, W., Ferguson, T. K., James, C. M., Krzycki, J. A., & Chan, M. K.
- Venue
- Science
- Published
- 2002-05-24
- Volume
- 296
- Issue
- 5572
- Pages
- 1462-1466
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2095370301
- Cited by
- 420
- References
- 18
- FWCI
- 16.14
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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