A conserved asparagine has a structural role in ubiquitin-conjugating enzymes.

ABSTRACT: 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.

SUBMITTER: Berndsen CE 

PROVIDER: S-EPMC3578109 | biostudies-literature | 2013 Mar

REPOSITORIES: biostudies-literature