5YZ1

Crystal structure of human Archease

5YZ1 の概要

• エントリーDOI: 10.2210/pdb5yz1/pdb
• 分子名称: Protein archease, DI(HYDROXYETHYL)ETHER, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: key cofacor, human rtcb, chaperone
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 43948.95

構造登録者

Duan, S.Y.,Li, J.X. (登録日: 2017-12-11, 公開日: 2019-01-02, 最終更新日: 2023-11-22)

主引用文献

Duan, S.,Gao, W.,Chen, Z.,Li, Z.,Li, S.,Gan, J.,Chen, X.,Li, J.
Crystal structure of human archease, a key cofactor of tRNA splicing ligase complex.
Int.J.Biochem.Cell Biol., 122:105744-105744, 2020

PubMed Abstract: The human archease, hereafter named HArch, is identified as a key cofactor of the tRNA-splicing ligase complex, and a potential therapeutic target for treating nervous system injuries. However, little is known about the structural basis of HArch in tRNA maturation, mRNA splicing, and RNA repair. Here we report the crystal structures of HArch and its two mutants D51A and D178A with resolutions ranging from 1.96 Å to 3.4 Å. HArch is composed of an extended N-terminal protrusion domain (NTD) and one compacted C-terminal domain (CTD). Unlike previously reported homologous proteins, the NTD of the first subunit interacts with the CTD of the second one, and this interaction might be important for maintaining protein stability. Moreover, HArch interacts and colocalizes with RNA ligase RTCB in cells. Our current study reveals the atomic structure of HArch and may help us understand its function in mRNA splicing.

PubMed: 32234548
DOI: 10.1016/j.biocel.2020.105744

実験手法

X-RAY DIFFRACTION (1.97 Å)