2AAK

UBIQUITIN CONJUGATING ENZYME FROM ARABIDOPSIS THALIANA

「1AAK」から置き換えられました

2AAK の概要

• エントリーDOI: 10.2210/pdb2aak/pdb
• 分子名称: UBIQUITIN CONJUGATING ENZYME (1 entity in total)
• 機能のキーワード: ubiquitin conjugation, ligase
• 由来する生物種: Arabidopsis thaliana (thale cress)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17298.38

構造登録者

Cook, W.J.,Jeffrey, L.C.,Sullivan, M.L.,Vierstra, R.D. (登録日: 1997-11-06, 公開日: 1998-03-18, 最終更新日: 2024-02-14)

主引用文献

Cook, W.J.,Jeffrey, L.C.,Sullivan, M.L.,Vierstra, R.D.
Three-dimensional structure of a ubiquitin-conjugating enzyme (E2).
J.Biol.Chem., 267:15116-15121, 1992

PubMed Abstract: The x-ray crystal structure of a recombinant ubiquitin-conjugating enzyme (E2) encoded by the UBC1 gene of the plant Arabidopsis thaliana has been determined with the use of multiple isomorphous replacement techniques and refined at 2.4-A resolution by simulated annealing and restrained least-squares. This E2 is an alpha/beta protein, with four alpha-helices and a four-stranded antiparallel beta-sheet. The NH2 and COOH termini, which may be important for interaction with other enzymes and substrates in the ubiquitin-conjugation pathway, are on the opposite side of the molecule from the cysteine residue that binds to the COOH terminus of ubiquitin. This structure should now allow for the rational analysis of E2 function by in vitro mutagenesis and facilitate the effective design of E2s with unique specificities or catalytic functions.

PubMed: 1321826

実験手法

X-RAY DIFFRACTION (2.4 Å)