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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Alanyl-tRNA synthetase crystal structure and design for acceptor-stem recognition.

Early work on aminoacylation of alanine-specific tRNA (tRNA(Ala)) by alanyl-tRNA synthetase (AlaRS) gave rise to the concept of an early "second genetic code" imbedded in the acceptor stems of tRNAs. A single conserved and position-specific G:U base pair in the tRNA acceptor stem is the key identity determinant. Further understanding has been limited due to lack of a crystal structure of the enzyme. We determined a 2.14 A crystal structure of the 453 amino acid catalytic fragment of Aquifex aeolicus AlaRS. It contains the catalytic domain characteristic of class II synthetases, a helical domain with a hairpin motif critical for acceptor-stem recognition, and a C-terminal domain of a mixed alpha/beta fold. Docking of tRNA(Ala) on AlaRS shows critical contacts with the three domains, consistent with previous mutagenesis and functional data. It also suggests conformational flexibility within the C domain, which might allow for the positional variation of the key G:U base pair seen in some tRNA(Ala)s.[1]

References

  1. Alanyl-tRNA synthetase crystal structure and design for acceptor-stem recognition. Swairjo, M.A., Otero, F.J., Yang, X.L., Lovato, M.A., Skene, R.J., McRee, D.E., Ribas de Pouplana, L., Schimmel, P. Mol. Cell (2004) [Pubmed]
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