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

ABSTRACT

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.

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