It is widely accepted that ubiquitin conjugating enzymes (E2) contain an active site asparagine that serves as an oxyanion hole, thereby stabilizing a negatively charged transition state intermediate and promoting ubiquitin transfer. Using structural and biochemical approaches to study the role of the conserved asparagine to ubiquitin conjugation by Ubc13/Mms2, we conclude that the importance of this residue stems primarily from its structural role in stabilizing an active site loop.
A conserved asparagine plays a structural role in ubiquitin-conjugating enzymes
Christopher E. Berndsen,R. Wiener,Ian Yu,A. Ringel,C. Wolberger
Published 2013 in Nature Chemical Biology
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- Publication year
2013
- Venue
Nature Chemical Biology
- Publication date
2013-01-03
- Fields of study
Biology, Medicine, Chemistry
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Semantic Scholar, PubMed
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