A conserved asparagine has a structural role in ubiquitin-conjugating enzymes.
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ABSTRACT:
SUBMITTER: Berndsen CE
PROVIDER: S-EPMC3578109 | biostudies-literature | 2013 Mar
REPOSITORIES: biostudies-literature
Publications
A conserved asparagine has a structural role in ubiquitin-conjugating enzymes.
Berndsen Christopher E CE Wiener Reuven R Yu Ian W IW Ringel Alison E AE Wolberger Cynthia C
Nature chemical biology 20130106 3
It is widely accepted that ubiquitin-conjugating enzymes 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. ...[more]
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