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

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.

Citation

Christopher E Berndsen, Reuven Wiener, Ian W Yu, Alison E Ringel, Cynthia Wolberger. A conserved asparagine has a structural role in ubiquitin-conjugating enzymes. Nature chemical biology. 2013 Mar;9(3):154-6

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PMID: 23292652

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