Ubiquitin transfer by a RING E3 ligase occurs from a closed E2~ubiquitin conformation

• Published in: Nature communications Vol. 11; no. 1; pp. 2846 - 11
• Main Authors: Branigan, Emma, Carlos Penedo, J., Hay, Ronald T.
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 05.06.2020; Nature Publishing Group; Nature Portfolio
• Subjects: 631/337/458/582; 631/45/173; 631/57/2265; Catalysis; Conformation; Conjugates; Crystallography, X-Ray; Efficiency; Energy transfer; Enzymes; Fluorescence Resonance Energy Transfer; Humanities and Social Sciences; Locking; multidisciplinary; Nuclear Proteins - metabolism; Protein Structure, Tertiary; Proteins; RING Finger Domains; Science; Science (multidisciplinary); Single Molecule Imaging; Structural analysis; Substrates; Transcription Factors - metabolism; Ubiquitin; Ubiquitin - metabolism; Ubiquitin-Conjugating Enzymes - metabolism; Ubiquitin-protein ligase; Ubiquitin-Protein Ligases - metabolism; Ubiquitination

Based on extensive structural analysis it was proposed that RING E3 ligases prime the E2~ubiquitin conjugate (E2~Ub) for catalysis by locking it into a closed conformation, where ubiquitin is folded back onto the E2 exposing the restrained thioester bond to attack by substrate nucleophile. However t...