3i7f

Publication Abstract from PubMed

The crystal structure of the aspartyl-tRNA synthetase from the eukaryotic parasite Entamoeba histolytica has been determined at 2.8Aresolution. Relative to homologous sequences, the E. histolytica protein contains a 43-residue insertion between the N-terminal anticodon binding domain and the C-terminal catalytic domain. The present structure reveals that this insertion extends an arm of the hinge region that has previously been shown to mediate interaction of aspartyl-tRNA synthetase with the cognate tRNA D-stem. Modeling indicates that this Entamoeba-specific insertion is likely to increase the interaction surface with the cognate tRNA(Asp). In doing so it may substitute functionally for an RNA-binding motif located in N-terminal extensions found in AspRS sequences from lower eukaryotes but absent in Entamoeba. The E. histolytica AspRS structure shows a well-ordered N-terminus that contributes to the AspRS dimer interface.

Crystal structure of the aspartyl-tRNA synthetase from Entamoeba histolytica.,Merritt EA, Arakaki TL, Larson ET, Kelley A, Mueller N, Napuli AJ, Zhang L, Deditta G, Luft J, Verlinde CL, Fan E, Zucker F, Buckner FS, Van Voorhis WC, Hol WG Mol Biochem Parasitol. 2010 Feb;169(2):95-100. Epub 2009 Oct 27. PMID:19874856^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.