Journal
STRUCTURE
Volume 18, Issue 1, Pages 138-147Publisher
CELL PRESS
DOI: 10.1016/j.str.2009.11.007
Keywords
-
Funding
- Grant-in-Aid for Scientific Research on Priority Area [18076003]
- Grant-in-Aid for Scientific Research on Innovative Areas [20107004]
- Grant-in-Aid for Scientific Research (B) [21370050]
- Ministry of Education, Culture, Sports, Science and Technology
- JSPS Research Fellowships
- Grants-in-Aid for Scientific Research [18076003, 20107004] Funding Source: KAKEN
Ask authors/readers for more resources
E2 ubiquitin-conjugating enzymes catalyze the attachment of ubiquitin to lysine residues of target proteins. The UbcH5b E2 enzyme has been shown to play a key role in the initiation of the ubiquitination of substrate proteins upon action of several E3 ligases. Here we have determined the 2.2 angstrom crystal structure of an intermediate of UbcH5b similar to ubiquitin (Ub) conjugate, which is assembled into an infinite spiral through the backside interaction. This active complex may provide multiple E2 active sites, enabling efficient ubiquitination of substrates. Indeed, biochemical assays support a model in which the self-assembled UbcH5b similar to Ub can serve as a bridge for the gap between the lysine residue of the substrate and the catalytic cysteine of E2.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available