4UP7

Crystal structure of Entamoeba histolytica lysyl-tRNA synthetase in complex with lysyl-adenylate

4UP7 の概要

• エントリーDOI: 10.2210/pdb4up7/pdb
• 関連するPDBエントリー: 4UP8 4UP9 4UPA
• 分子名称: LYSINE--TRNA LIGASE, ADENOSINE-5'-[LYSYL-PHOSPHATE] (2 entities in total)
• 機能のキーワード: ligase, aminoacylation
• 由来する生物種: ENTAMOEBA HISTOLYTICA
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 88216.61

構造登録者

Bonnefond, L.,Nureki, O. (登録日: 2014-06-14, 公開日: 2014-10-29, 最終更新日: 2024-01-10)

主引用文献

Bonnefond, L.,Castro De Moura, M.,Ribas De Pouplana, L.,Nureki, O.
Crystal Structures of Entamoeba Histolytica Lysyl-tRNA Synthetase Reveal Conformational Changes Upon Lysine Binding and a Specific Helix Bundle Domain.
FEBS Lett., 588:4478-, 2014

PubMed Abstract: The class II lysyl-tRNA synthetases (KRS) are conserved aminoacyl-tRNA synthetases that attach lysine to the cognate tRNA in a two-step mechanism. The enzyme from the parasitic protozoan Entamoeba histolytica was crystallized in the presence of small ligands to generate snapshots of the lysine-adenylate formation. The residues involved in lysine activation are highly conserved and the active site closes around the lysyl-adenylate, as observed in bacterial KRS. The Entamoeba EMAPII-like polypeptide is not resolved in the crystals, but another Entamoeba-specific insertion could be modeled as a small helix bundle that may contribute to tRNA binding through interaction with the tRNA hinge.

PubMed: 25448989
DOI: 10.1016/J.FEBSLET.2014.10.019

実験手法

X-RAY DIFFRACTION (2.789 Å)