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

被引：0
|
作者：
Berndsen C.E. [1 ,2 ,3 ]
Wiener R. [1 ,2 ]
Yu I.W. [1 ]
Ringel A.E. [1 ]
Wolberger C. [1 ,2 ]
机构：
[1] Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD
[2] Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, MD
[3] Department of Chemistry and Biochemistry, James Madison University, Harrisonburg, VA
来源：
Nature Chemical Biology | 2013年 / 9卷 / 3期
基金：
美国国家科学基金会;
关键词：
D O I：
10.1038/nchembio.1159
中图分类号：
学科分类号：
摘要：
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. © 2013 Nature America, Inc. All rights reserved.
引用
收藏
页码：154 / 156
页数：2
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