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

Christopher E. Berndsen, Reuven Wiener, Ian W. Yu, Alison E. Ringel, Cynthia Wolberger

Research output: Contribution to journalArticle

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.

Original languageEnglish (US)
Pages (from-to)154-156
Number of pages3
JournalNature chemical biology
Volume9
Issue number3
DOIs
StatePublished - Mar 1 2013

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'A conserved asparagine has a structural role in ubiquitin-conjugating enzymes'. Together they form a unique fingerprint.

  • Cite this