4JFA
Crystal Structure of Plasmodium falciparum Tryptophanyl-tRNA synthetase
Summary for 4JFA
Entry DOI | 10.2210/pdb4jfa/pdb |
Related | 2AZX 2QUH |
Descriptor | Tryptophan--tRNA ligase, TRYPTOPHAN, BETA-MERCAPTOETHANOL, ... (5 entities in total) |
Functional Keywords | wrs, trprs, plasmodium, ligase |
Biological source | Plasmodium falciparum |
Total number of polymer chains | 4 |
Total formula weight | 196439.42 |
Authors | Khan, S.,Garg, A.,Manickam, Y.,Sharma, A. (deposition date: 2013-02-28, release date: 2014-01-29, Last modification date: 2025-03-26) |
Primary citation | Khan, S.,Garg, A.,Sharma, A.,Camacho, N.,Picchioni, D.,Saint-Leger, A.,Ribas de Pouplana, L.,Yogavel, M.,Sharma, A. An appended domain results in an unusual architecture for malaria parasite tryptophanyl-tRNA synthetase Plos One, 8:e66224-e66224, 2013 Cited by PubMed 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. PubMed: 23776638DOI: 10.1371/journal.pone.0066224 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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