Catalytic mechanism of the tryptophan activation reaction revealed by crystal structures of human tryptophanyl-tRNA synthetase in different enzymatic states

Human tryptophanyl-tRNA synthetase (hTrpRS) differs from its bacterial counterpart at several key positions of the catalytic active site and has an extra N-terminal domain, implying possibly a different catalytic mechanism. We report here the crystal structures of hTrpRS in complexes with Trp, trypt...

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Bibliografische gegevens
Hoofdauteurs: Shen, Ning, Zhou, Minyu, Yang, Bei, Yu, Yadong, Dong, Xianchi, Ding, Jianping
Formaat: Artigo
Taal:Inglês
Gepubliceerd in: Oxford University Press 2008
Onderwerpen:
Structural Biology
Online toegang:https://ncbi.nlm.nih.gov/pmc/articles/PMC2275098/
https://ncbi.nlm.nih.gov/pubmed/18180246
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1093/nar/gkm1153
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