4jfa

Publication Abstract from PubMed

Specific activation of amino acids by aminoacyl-tRNA synthetases (aaRSs) is essential for maintaining fidelity during protein translation. Here, we present crystal structure of malaria parasite Plasmodium falciparum tryptophanyl-tRNA synthetase (Pf-WRS) catalytic domain (AAD) at 2.6 A resolution in complex with L-tryptophan. Confocal microscopy-based localization data suggest cytoplasmic residency of this protein. Pf-WRS has an unusual N-terminal extension of AlaX-like domain (AXD) along with linker regions which together seem vital for enzymatic activity and tRNA binding. Pf-WRS is not proteolytically processed in the parasites and therefore AXD likely provides tRNA binding capability rather than editing activity. The N-terminal domain containing AXD and linker region is monomeric and would result in an unusual overall architecture for Pf-WRS where the dimeric catalytic domains have monomeric AXDs on either side. Our PDB-wide comparative analyses of 47 WRS crystal structures also provide new mechanistic insights into this enzyme family in context conserved KMSKS loop conformations.

An appended domain results in an unusual architecture for malaria parasite tryptophanyl-tRNA synthetase.,Khan S, Garg A, Sharma A, Camacho N, Picchioni D, Saint-Leger A, Ribas de Pouplana L, Yogavel M, Sharma A PLoS One. 2013 Jun 12;8(6):e66224. doi: 10.1371/journal.pone.0066224. Print 2013. PMID:23776638^[1]

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