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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Detalles Bibliográficos
Autores principales: Shen, Ning, Zhou, Minyu, Yang, Bei, Yu, Yadong, Dong, Xianchi, Ding, Jianping
Formato: Texto
Lenguaje:English
Publicado: Oxford University Press 2008
Materias:
Structural Biology
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2275098/
https://www.ncbi.nlm.nih.gov/pubmed/18180246
http://dx.doi.org/10.1093/nar/gkm1153

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2275098/
https://www.ncbi.nlm.nih.gov/pubmed/18180246
http://dx.doi.org/10.1093/nar/gkm1153

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