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Essentiality of a non-RING element in priming donor ubiquitin for catalysis by a monomeric E3

DOI: 10.1038/nsmb.2621 DOI Help
PMID: 23851457 PMID Help

Authors: Hao Dou (Beatson Institute for Cancer Research) , Lori Buetow (Beatson Institute for Cancer Research) , Gary J Sibbet (The Beatson Institute for Cancer Research, Glasgow) , Kenneth Cameron (Beatson Institute for Cancer Research) , Danny Huang (Beatson Institute for Cancer Research)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Structural & Molecular Biology , VOL 20 (8) , PAGES 982 - 986

State: Published (Approved)
Published: July 2013

Open Access Open Access

Abstract: RING E3 ligases catalyze the transfer of ubiquitin (Ub) from E2 ubiquitin-conjugating enzyme thioesterified with Ub (E2~Ub) to substrate. For RING E3 dimers, the RING domain of one subunit and tail of the second cooperate to prime Ub, but how this is accomplished by monomeric RING E3s in the absence of a tail-like component is currently unknown.

Journal Keywords: Signal; Amino; Crystallization; Humans; Kinetics; Magnetic; Models; Molecular; Phosphorylation; Protein; Proto-Oncogene; Sequence; Ubiquitin; Ubiquitin-Conjugating Enzymes

Subject Areas: Biology and Bio-materials

Instruments: I04-Macromolecular Crystallography , I24-Microfocus Macromolecular Crystallography

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