Crystal structure of the Aspartyl-tRNA synthetase from Entamoeba histolytica

The crystal structure of the aspartyl-tRNA synthetase from the eukaryotic parasite Entamoeba histolytica has been determined at 2.8 Å resolution. Relative to homologous sequences, the E. histolytica protein contains a 43-residue insertion between the N-terminal anticodon binding domain and the C-ter...

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Hlavní autoři: Merritt, Ethan A, Arakaki, Tracy L, Larson, Eric T, Kelley, Angela, Mueller, Natascha, Napuli, Alberto J, Zhang, Li, DeDitta, George, Luft, Joseph, Verlinde, Christophe L M J, Fan, Erkang, Zucker, Frank, Buckner, Frederick S, Van Voorhis, Wesley C, Hol, Wim G J
Médium: Artigo
Jazyk:Inglês
Vydáno: 2009
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Article
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC2791181/
https://ncbi.nlm.nih.gov/pubmed/19874856
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.molbiopara.2009.10.005
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