4P22

Crystal Structure of N-terminal Fragments of E1

4P22 の概要

• エントリーDOI: 10.2210/pdb4p22/pdb
• 分子名称: Ubiquitin-like modifier-activating enzyme 1 (2 entities in total)
• 機能のキーワード: e1, ubiquitin, ligase
• 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: 96915.84

構造登録者

Xie, S.-T. (登録日: 2014-02-28, 公開日: 2015-02-25, 最終更新日: 2023-12-27)

主引用文献

Xie, S.T.
Expression, purification, and crystal structure of N-terminal domains of human ubiquitin-activating enzyme (E1).
Biosci.Biotechnol.Biochem., 78:1542-1549, 2014

PubMed Abstract: Ubiquitin-activating enzyme (E1) is a key regulator in protein ubiquitination, which lies on the upstream of the ubiquitin-related pathways and determines the activation of the downstream enzyme cascade. Thus far, no structural information about the human ubiquitin-activating enzyme has been reported. We expressed and purified the N-terminal domains of human E1 and determined their crystal structures, which contain inactive adenylation domain (IAD) and the first catalytic cysteine half-domain (FCCH). This study presents the crystal structure of human E1 fragment for the first time. The main structure of both IAD and FCCH superimposed well with their corresponding domains in yeast Uba1, but their relative positions vary significantly. This work provides new structural insights in understanding the mechanisms of ubiquitin activation in humans.

PubMed: 25209502
DOI: 10.1080/09168451.2014.923301

実験手法

X-RAY DIFFRACTION (2.75 Å)