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Nat Chem Biol. 2013 Mar;9(3):154-6. doi: 10.1038/nchembio.1159. Epub 2013 Jan 6.

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

Author information

1
Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA.

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.

PMID:
23292652
PMCID:
PMC3578109
DOI:
10.1038/nchembio.1159
[Indexed for MEDLINE]
Free PMC Article

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