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Nature Research, Nature Chemical Biology, 3(9), p. 154-156, 2013

DOI: 10.1038/nchembio.1159

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

Journal article published in 2013 by Christopher E. Berndsen, Reuven Wiener, Ian W. Yu, Alison E. Ringel, Cynthia Wolberger ORCID
This paper was not found in any repository, but could be made available legally by the author.
This paper was not found in any repository, but could be made available legally by the author.

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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.