3I7F

Aspartyl tRNA synthetase from Entamoeba histolytica

Summary for 3I7F

• Entry DOI: 10.2210/pdb3i7f/pdb
• Descriptor: Aspartyl-tRNA synthetase (2 entities in total)
• Functional Keywords: trna ligase, apo, atp-binding, aminoacyl-trna synthetase, ligase, nucleotide-binding, protein biosynthesis, structural genomics, medical structural genomics of pathogenic protozoa, msgpp
• Biological source: Entamoeba histolytica
• Total number of polymer chains: 2
• Total formula weight: 125951.47

Authors

Arakaki, T.,Merritt, E.A.,Medical Structural Genomics of Pathogenic Protozoa (MSGPP) (deposition date: 2009-07-08, release date: 2009-07-21, Last modification date: 2024-02-21)

Primary citation

Merritt, E.A.,Arakaki, T.L.,Larson, E.T.,Kelley, A.,Mueller, N.,Napuli, A.J.,Zhang, L.,Deditta, G.,Luft, J.,Verlinde, C.L.,Fan, E.,Zucker, F.,Buckner, F.S.,Van Voorhis, W.C.,Hol, W.G.
Crystal structure of the aspartyl-tRNA synthetase from Entamoeba histolytica.
Mol.Biochem.Parasitol., 169:95-100, 2010

PubMed Abstract: 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.

PubMed: 19874856
DOI: 10.1016/j.molbiopara.2009.10.005

Experimental method

X-RAY DIFFRACTION (2.8 Å)