3PZ6

The crystal structure of GlLeuRS-CP1

3PZ6 の概要

• エントリーDOI: 10.2210/pdb3pz6/pdb
• 関連するPDBエントリー: 3PZ0 3PZ5
• 分子名称: Leucyl-tRNA synthetase (2 entities in total)
• 機能のキーワード: editing domain, glleurs_cp1, ligase
• 由来する生物種: Giardia intestinalis (Giardia lamblia)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 208140.80

構造登録者

Liu, R.J.,Du, D.H.,Wang, E.D. (登録日: 2010-12-14, 公開日: 2011-08-24, 最終更新日: 2023-11-01)

主引用文献

Liu, R.J.,Tan, M.,Du, D.H.,Xu, B.S.,Eriani, G.,Wang, E.D.
Peripheral insertion modulates the editing activity of the isolated CP1 domain of leucyl-tRNA synthetase
Biochem.J., 440:217-227, 2011

PubMed Abstract: A large insertion domain called CP1 (connective peptide 1) present in class Ia aminoacyl-tRNA synthetases is responsible for post-transfer editing. LeuRS (leucyl-tRNA synthetase) from Aquifex aeolicus and Giardia lamblia possess unique 20 and 59 amino acid insertions respectively within the CP1 that are crucial for editing activity. Crystal structures of AaLeuRS-CP1 [2.4 Å (1 Å=0.1 nm)], GlLeuRS-CP1 (2.6 Å) and the insertion deletion mutant AaLeuRS-CP1Δ20 (2.5 Å) were solved to understand the role of these insertions in editing. Both insertions are folded as peripheral motifs located on the opposite side of the proteins from the active-site entrance in the CP1 domain. Docking modelling and site-directed mutagenesis showed that the insertions do not interact with the substrates. Results of molecular dynamics simulations show that the intact CP1 is more dynamic than its mutant devoid of the insertion motif. Taken together, the data show that a peripheral insertion without a substrate-binding site or major structural role in the active site may modulate catalytic function of a protein, probably from protein dynamics regulation in two respective LeuRS CP1s. Further results from proline and glycine mutational analyses intended to reduce or increase protein flexibility are consistent with this hypothesis.

PubMed: 21819379
DOI: 10.1042/BJ20111177

実験手法

X-RAY DIFFRACTION (2.6 Å)