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An Appended Domain Results in an Unusual Architecture for Malaria Parasite Tryptophanyl-tRNA Synthetase
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...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3680381/ https://www.ncbi.nlm.nih.gov/pubmed/23776638 http://dx.doi.org/10.1371/journal.pone.0066224 |
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author | Khan, Sameena Garg, Ankur Sharma, Arvind Camacho, Noelia Picchioni, Daria Saint-Léger, Adélaïde de Pouplana, Lluís Ribas Yogavel, Manickam Sharma, Amit |
author_facet | Khan, Sameena Garg, Ankur Sharma, Arvind Camacho, Noelia Picchioni, Daria Saint-Léger, Adélaïde de Pouplana, Lluís Ribas Yogavel, Manickam Sharma, Amit |
author_sort | Khan, Sameena |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-3680381 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-36803812013-06-17 An Appended Domain Results in an Unusual Architecture for Malaria Parasite Tryptophanyl-tRNA Synthetase Khan, Sameena Garg, Ankur Sharma, Arvind Camacho, Noelia Picchioni, Daria Saint-Léger, Adélaïde de Pouplana, Lluís Ribas Yogavel, Manickam Sharma, Amit PLoS One Research Article 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. Public Library of Science 2013-06-12 /pmc/articles/PMC3680381/ /pubmed/23776638 http://dx.doi.org/10.1371/journal.pone.0066224 Text en © 2013 Khan et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Khan, Sameena Garg, Ankur Sharma, Arvind Camacho, Noelia Picchioni, Daria Saint-Léger, Adélaïde de Pouplana, Lluís Ribas Yogavel, Manickam Sharma, Amit An Appended Domain Results in an Unusual Architecture for Malaria Parasite Tryptophanyl-tRNA Synthetase |
title | An Appended Domain Results in an Unusual Architecture for Malaria Parasite Tryptophanyl-tRNA Synthetase |
title_full | An Appended Domain Results in an Unusual Architecture for Malaria Parasite Tryptophanyl-tRNA Synthetase |
title_fullStr | An Appended Domain Results in an Unusual Architecture for Malaria Parasite Tryptophanyl-tRNA Synthetase |
title_full_unstemmed | An Appended Domain Results in an Unusual Architecture for Malaria Parasite Tryptophanyl-tRNA Synthetase |
title_short | An Appended Domain Results in an Unusual Architecture for Malaria Parasite Tryptophanyl-tRNA Synthetase |
title_sort | appended domain results in an unusual architecture for malaria parasite tryptophanyl-trna synthetase |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3680381/ https://www.ncbi.nlm.nih.gov/pubmed/23776638 http://dx.doi.org/10.1371/journal.pone.0066224 |
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