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

It is widely accepted that ubiquitin conjugating enzymes (E2) 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 t...

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Autores principales: Berndsen, Christopher E., Wiener, Reuven, Yu, Ian W., Ringel, Alison E., Wolberger, Cynthia
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2013
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3578109/
https://www.ncbi.nlm.nih.gov/pubmed/23292652
http://dx.doi.org/10.1038/nchembio.1159
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author Berndsen, Christopher E.
Wiener, Reuven
Yu, Ian W.
Ringel, Alison E.
Wolberger, Cynthia
author_facet Berndsen, Christopher E.
Wiener, Reuven
Yu, Ian W.
Ringel, Alison E.
Wolberger, Cynthia
author_sort Berndsen, Christopher E.
collection PubMed
description It is widely accepted that ubiquitin conjugating enzymes (E2) 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.
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spelling pubmed-35781092013-09-01 A conserved asparagine plays a structural role in ubiquitin-conjugating enzymes Berndsen, Christopher E. Wiener, Reuven Yu, Ian W. Ringel, Alison E. Wolberger, Cynthia Nat Chem Biol Article It is widely accepted that ubiquitin conjugating enzymes (E2) 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. 2013-01-06 2013-03 /pmc/articles/PMC3578109/ /pubmed/23292652 http://dx.doi.org/10.1038/nchembio.1159 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Berndsen, Christopher E.
Wiener, Reuven
Yu, Ian W.
Ringel, Alison E.
Wolberger, Cynthia
A conserved asparagine plays a structural role in ubiquitin-conjugating enzymes
title A conserved asparagine plays a structural role in ubiquitin-conjugating enzymes
title_full A conserved asparagine plays a structural role in ubiquitin-conjugating enzymes
title_fullStr A conserved asparagine plays a structural role in ubiquitin-conjugating enzymes
title_full_unstemmed A conserved asparagine plays a structural role in ubiquitin-conjugating enzymes
title_short A conserved asparagine plays a structural role in ubiquitin-conjugating enzymes
title_sort conserved asparagine plays a structural role in ubiquitin-conjugating enzymes
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3578109/
https://www.ncbi.nlm.nih.gov/pubmed/23292652
http://dx.doi.org/10.1038/nchembio.1159
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