Structural highlights
Function
[UBC13_YEAST] Has a role in the DNA error-free postreplication repair (PRR) pathway. The UBC13/MMS2 heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through 'Lys-63'.
Publication Abstract from PubMed
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.
A conserved asparagine has a structural role in ubiquitin-conjugating enzymes.,Berndsen CE, Wiener R, Yu IW, Ringel AE, Wolberger C Nat Chem Biol. 2013 Mar;9(3):154-6. doi: 10.1038/nchembio.1159. Epub 2013 Jan 6. PMID:23292652[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Berndsen CE, Wiener R, Yu IW, Ringel AE, Wolberger C. A conserved asparagine has a structural role in ubiquitin-conjugating enzymes. Nat Chem Biol. 2013 Mar;9(3):154-6. doi: 10.1038/nchembio.1159. Epub 2013 Jan 6. PMID:23292652 doi:10.1038/nchembio.1159
