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3HRI

Histidyl-tRNA synthetase (apo) from Trypanosoma brucei

3HRI の概要
エントリーDOI10.2210/pdb3hri/pdb
関連するPDBエントリー3HRJ 3HRK
分子名称Histidyl-tRNA synthetase (1 entity in total)
機能のキーワードapo trna-ligase, aminoacyl-trna synthetase, ligase, structural genomics, medical structural genomics of pathogenic protozoa, msgpp
由来する生物種Trypanosoma brucei
タンパク質・核酸の鎖数6
化学式量合計307245.73
構造登録者
Arakaki, T.L.,Merritt, E.A.,Larson, E.T.,Medical Structural Genomics of Pathogenic Protozoa (MSGPP) (登録日: 2009-06-09, 公開日: 2009-12-01, 最終更新日: 2024-04-03)
主引用文献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: 20132829
DOI: 10.1016/j.jmb.2010.01.051
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.85 Å)
構造検証レポート
Validation report summary of 3hri
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-12-31に公開中

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