Summary for 3LC0
| Entry DOI | 10.2210/pdb3lc0/pdb |
| Related | 3hri 3hrk |
| Descriptor | Histidyl-tRNA synthetase, HISTIDINE (3 entities in total) |
| Functional Keywords | trna-ligase, aminoacyl-trna synthetase, ligase, structural genomics, medical structural genomics of pathogenic protozoa, msgpp |
| Biological source | Trypanosoma cruzi |
| Total number of polymer chains | 1 |
| Total formula weight | 51341.75 |
| Authors | Merritt, E.A.,Larson, E.T.,Medical Structural Genomics of Pathogenic Protozoa (MSGPP) (deposition date: 2010-01-08, release date: 2010-01-19, Last modification date: 2024-02-21) |
| Primary citation | Merritt, E.A.,Arakaki, T.L.,Gillespie, J.R.,Larson, E.T.,Kelley, A.,Mueller, N.,Napuli, A.J.,Kim, J.,Zhang, L.,Verlinde, C.L.,Fan, E.,Zucker, F.,Buckner, F.S.,Van Voorhis, W.C.,Hol, W.G. Crystal Structures of Trypanosomal Histidyl-tRNA Synthetase Illuminate Differences between Eukaryotic and Prokaryotic Homologs. J.Mol.Biol., 397:481-494, 2010 Cited by PubMed 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. PubMed: 20132829DOI: 10.1016/j.jmb.2010.01.051 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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