1FZY

CRYSTAL STRUCTURE OF SACCHAROMYCES CEREVISIAE UBIQUITIN CONJUGATING ENZYME 1

1FZY の概要

• エントリーDOI: 10.2210/pdb1fzy/pdb
• 分子名称: UBIQUITIN-CONJUGATING ENZYME E2-24 KDA (2 entities in total)
• 機能のキーワード: alpha-beta roll, ligase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 33394.13

構造登録者

Glover, M.,Williams, R.S. (登録日: 2000-10-04, 公開日: 2001-10-04, 最終更新日: 2024-02-07)

主引用文献

Hamilton, K.S.,Ellison, M.J.,Barber, K.R.,Williams, R.S.,Huzil, J.T.,McKenna, S.,Ptak, C.,Glover, M.,Shaw, G.S.
Structure of a conjugating enzyme-ubiquitin thiolester intermediate reveals a novel role for the ubiquitin tail.
Structure, 9:897-904, 2001

PubMed Abstract: Ubiquitin-conjugating enzymes (E2s) are central enzymes involved in ubiquitin-mediated protein degradation. During this process, ubiquitin (Ub) and the E2 protein form an unstable E2-Ub thiolester intermediate prior to the transfer of ubiquitin to an E3-ligase protein and the labeling of a substrate for degradation. A series of complex interactions occur among the target substrate, ubiquitin, E2, and E3 in order to efficiently facilitate the transfer of the ubiquitin molecule. However, due to the inherent instability of the E2-Ub thiolester, the structural details of this complex intermediate are not known.

PubMed: 11591345
DOI: 10.1016/S0969-2126(01)00657-8

実験手法

X-RAY DIFFRACTION (1.9 Å)