ArticlePloS one2013
An appended domain results in an unusual architecture for malaria parasite tryptophanyl-tRNA synthetase.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 25 citations in OpenAlex.
- Structural analyses of the malaria parasite aminoacyl-tRNA synthetases provide new avenues for antimalarial drug discovery.Protein science : a publication of the Protein Society · 2021Review
- A Fifth of the Protein World: Rossmann-like Proteins as an Evolutionarily Successful Structural unit.Journal of molecular biology · 2021Article
- Aminoacyl tRNA synthetases as malarial drug targets: a comparative bioinformatics study.Malaria journal · 2019Article
- Protein Translation Enzyme lysyl-tRNA Synthetase Presents a New Target for Drug Development against Causative Agents of Loiasis and Schistosomiasis.PLoS neglected tropical diseases · 2016Article
- Selective inhibition of apicoplast tryptophanyl-tRNA synthetase causes delayed death in Plasmodium falciparum.Scientific reports · 2016Article
- Recent advances in the biology and drug targeting of malaria parasite aminoacyl-tRNA synthetases.Malaria journal · 2016Review
- Structural and functional attributes of malaria parasite diadenosine tetraphosphate hydrolase.Scientific reports · 2016Article
- Structural and functional analysis of the anti-malarial drug target prolyl-tRNA synthetase.Journal of structural and functional genomics · 2014Article
- Structural basis of malaria parasite lysyl-tRNA synthetase inhibition by cladosporin.Journal of structural and functional genomics · 2014Article
- Conformational landscapes for KMSKS loop in tyrosyl-tRNA synthetases.Journal of structural and functional genomics · 2014Article
- Aminoacyl-tRNA synthetases as drug targets in eukaryotic parasites.International journal for parasitology. Drugs and drug resistance · 2014Review
- A nondiscriminating glutamyl-tRNA synthetase in the plasmodium apicoplast: the first enzyme in an indirect aminoacylation pathway.The Journal of biological chemistry · 2013Article
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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 Å 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.
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