ArticleJournal of molecular biology2010
Crystal structures of trypanosomal histidyl-tRNA synthetase illuminate differences between eukaryotic and prokaryotic homologs.
Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 40 citations in OpenAlex.
- Aminoacyl tRNA Synthetases: Implications of Structural Biology in Drug Development against Trypanosomatid Parasites.ACS omega · 2023Review
- Synthesis of new N,S-acetal analogs derived from juglone with cytotoxic activity against Trypanossoma cruzi.Journal of bioenergetics and biomembranes · 2020Article
- Targeting tRNA-synthetase interactions towards novel therapeutic discovery against eukaryotic pathogens.PLoS neglected tropical diseases · 2020Article
- Proteomic analysis of the second-generation merozoites of Eimeria tenella under nitromezuril and ethanamizuril stress.Parasites & vectors · 2019Article
- Backbone Brackets and Arginine Tweezers delineate Class I and Class II aminoacyl tRNA synthetases.PLoS computational biology · 2018Article
- Identification of Chemical Compounds That Inhibit the Function of Histidyl-tRNA Synthetase from Pseudomonas aeruginosa.SLAS discovery : advancing life sciences R & D · 2018Article
- The Usher Syndrome Type IIIB Histidyl-tRNA Synthetase Mutation Confers Temperature Sensitivity.Biochemistry · 2017Article
- Ligand co-crystallization of aminoacyl-tRNA synthetases from infectious disease organisms.Scientific reports · 2017Article
- The Potential of Secondary Metabolites from Plants as Drugs or Leads against Protozoan Neglected Diseases-Part III: In-Silico Molecular Docking Investigations.Molecules (Basel, Switzerland) · 2016Review
- Aminoacyl-tRNA Synthetases in the Bacterial World.EcoSal Plus · 2016Review
- A binding hotspot in Trypanosoma cruzi histidyl-tRNA synthetase revealed by fragment-based crystallographic cocktail screens.Acta crystallographica. Section D, Biological crystallography · 2015Article
- Structural basis for recognition of G-1-containing tRNA by histidyl-tRNA synthetase.Nucleic acids research · 2015Article
- Interaction between the tRNA-binding and C-terminal domains of Yeast Gcn2 regulates kinase activity in vivo.PLoS genetics · 2015Article
- Comparison of histidine recognition in human and trypanosomatid histidyl-tRNA synthetases.Biochimie · 2014Article
- Genetic validation of aminoacyl-tRNA synthetases as drug targets in Trypanosoma brucei.Eukaryotic cell · 2014Article
- Emergence and evolution.Topics in current chemistry · 2014Review
- Crystal structures of Plasmodium falciparum cytosolic tryptophanyl-tRNA synthetase and its potential as a target for structure-guided drug design.Molecular and biochemical parasitology · 2013Article
- Unusual domain architecture of aminoacyl tRNA synthetases and their paralogs from Leishmania major.BMC genomics · 2012Article
- New WS9326A congeners from Streptomyces sp. 9078 inhibiting Brugia malayi asparaginyl-tRNA synthetase.Organic letters · 2012Article
- Internally deleted human tRNA synthetase suggests evolutionary pressure for repurposing.Structure (London, England : 1993) · 2012Article
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Authors and funding
15 authors at 2 institutions in 1 country.
Funding
Abstract
Crystal structures of histidyl-tRNA synthetase (HisRS) from the eukaryotic parasites Trypanosoma brucei and Trypanosoma cruzi provide a first structural view of a eukaryotic form of this enzyme and reveal differences from bacterial homologs. HisRSs in general contain an extra domain inserted between conserved motifs 2 and 3 of the Class II aminoacyl-tRNA synthetase catalytic core. The current structures show that the three-dimensional topology of this domain is very different in bacterial and archaeal/eukaryotic forms of the enzyme. Comparison of apo and histidine-bound trypanosomal structures indicates substantial active-site rearrangement upon histidine binding but relatively little subsequent rearrangement after reaction of histidine with ATP to form the enzyme's first reaction product, histidyladenylate. The specific residues involved in forming the binding pocket for the adenine moiety differ substantially both from the previously characterized binding site in bacterial structures and from the homologous residues in human HisRSs. The essentiality of the single HisRS gene in T. brucei is shown by a severe depression of parasite growth rate that results from even partial suppression of expression by RNA interference.
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