title: A conserved asparagine has a structural role in ubiquitin-conjugating enzymes.
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.
authors.affiliation: Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA.
authors.forename: Christopher E
authors.initials: CE
authors.lastname: Berndsen
authors.forename: Reuven
authors.initials: R
authors.lastname: Wiener
authors.forename: Ian W
authors.initials: IW
authors.lastname: Yu
authors.forename: Alison E
authors.initials: AE
authors.lastname: Ringel
authors.forename: Cynthia
authors.initials: C
authors.lastname: Wolberger
mesh_terms: D001216:Asparagine / Q000737:chemistry / Q000378:metabolism*; D020134:Catalytic Domain; D017124:Conserved Sequence; D008958:Models, Molecular; D011487:Protein Conformation; D025801:Ubiquitin / Q000378:metabolism; D044763:Ubiquitin-Conjugating Enzymes / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D025801:Ubiquitin; D001216:Asparagine; D044763:Ubiquitin-Conjugating Enzymes