4RDX

Structure of histidinyl-tRNA synthetase in complex with tRNA(His)

4RDX の概要

• エントリーDOI: 10.2210/pdb4rdx/pdb
• 分子名称: Histidine--tRNA ligase, tRNA(his), ADENOSINE MONOPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: aminoacyl-trna synthetase, classii aars, aminoacylation, histidine, trna, ligase-rna complex, ligase/rna
• 由来する生物種: Thermus thermophilus HB27; 詳細
• 細胞内の位置: Cytoplasm : P62374
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 73095.40

構造登録者

Xie, W.,Tian, Q.,Wang, C. (登録日: 2014-09-20, 公開日: 2015-03-25, 最終更新日: 2023-11-08)

主引用文献

Tian, Q.,Wang, C.,Liu, Y.,Xie, W.
Structural basis for recognition of G-1-containing tRNA by histidyl-tRNA synthetase
Nucleic Acids Res., 43:2980-2990, 2015

PubMed Abstract: Aminoacyl-tRNA synthetases (aaRSs) play a crucial role in protein translation by linking tRNAs with cognate amino acids. Among all the tRNAs, only tRNA(His) bears a guanine base at position -1 (G-1), and it serves as a major recognition element for histidyl-tRNA synthetase (HisRS). Despite strong interests in the histidylation mechanism, the tRNA recognition and aminoacylation details are not fully understood. We herein present the 2.55 Å crystal structure of HisRS complexed with tRNA(His), which reveals that G-1 recognition is principally nonspecific interactions on this base and is made possible by an enlarged binding pocket consisting of conserved glycines. The anticodon triplet makes additional specific contacts with the enzyme but the rest of the loop is flexible. Based on the crystallographic and biochemical studies, we inferred that the uniqueness of histidylation system originates from the enlarged binding pocket (for the extra base G-1) on HisRS absent in other aaRSs, and this structural complementarity between the 5' extremity of tRNA and enzyme is probably a result of coevolution of both.

PubMed: 25722375
DOI: 10.1093/nar/gkv129

実験手法

X-RAY DIFFRACTION (2.55 Å)