The 2 Å crystal structure of leucyl-tRNA synthetase and its complex with a leucyl-adenylate analogue

Leucyl-, isoleucyl- and valyl-tRNA synthetases are closely related large monomeric class I synthetases. Each contains a homologous insertion domain of ∼200 residues, which is thought to permit them to hydrolyse (‘edit’) cognate tRNA that has been mischarged with a chemically similar but non-cognate...

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Vydáno v:	EMBO J
Hlavní autoři:	Cusack, Stephen, Yaremchuk, Anna, Tukalo, Michael
Médium:	Artigo
Jazyk:	Inglês
Vydáno:	Nature Publishing Group 2000
Témata:	Articles
On-line přístup:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC384370/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/10811626/ https://ncbi.nlm.nih.govhttps://doi.org/10.1093/emboj/19.10.2351
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