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- Title
Crystal structure of the human ubiquitin conjugating enzyme complex, hMms2-hUbc13.
- Authors
Moraes, T F; Edwards, R A; McKenna, S; Pastushok, L; Xiao, W; Glover, J N; Ellison, M J
- Abstract
The ubiquitin conjugating enzyme complex Mms2-Ubc13 plays a key role in post-replicative DNA repair in yeast and the NF-kappaB signal transduction pathway in humans. This complex assembles novel polyubiquitin chains onto yet uncharacterized protein targets. Here we report the crystal structure of a complex between hMms2 (Uev1) and hUbc13 at 1.85 A resolution and a structure of free hMms2 at 1.9 A resolution. These structures reveal that the hMms2 monomer undergoes a localized conformational change upon interaction with hUbc13. The nature of the interface provides a physical basis for the preference of Mms2 for Ubc13 as a partner over a variety of other structurally similar ubiquitin-conjugating enzymes. The structure of the hMms2-hUbc13 complex provides the conceptual foundation for understanding the mechanism of Lys 63 multiubiquitin chain assembly and for its interactions with the RING finger proteins Rad5 and Traf6.
- Publication
Nature structural biology, 2001, Vol 8, Issue 8, p669
- ISSN
1072-8368
- Publication type
Journal Article
- DOI
10.1038/90373