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

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

doi:10.1038/nchembio.1159

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 journal › Article › peer-review

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 language	English
Pages (from-to)	154-156
Number of pages	3
Journal	Nature Chemical Biology
Volume	9
Issue number	3
DOIs	https://doi.org/10.1038/nchembio.1159
State	Published - Mar 2013
Externally published	Yes

All Science Journal Classification (ASJC) codes

Molecular Biology
Cell Biology

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10.1038/nchembio.1159

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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.",

author = "Berndsen, \{Christopher E.\} and Reuven Wiener and Yu, \{Ian W.\} and Ringel, \{Alison E.\} and Cynthia Wolberger",

note = "Funding Information: We thank J. Hurley (National Institute of Diabetes and Digestive and Kidney Diseases) for the Ubc13–Mms2 coexpression plasmid and X. Zhang (Johns Hopkins University) for human E1 protein. We also thank J. Stivers, A. Hengge and L. Spyracopoulos for helpful discussions. This work was supported in part by a grant from the US National Science Foundation (MCB-0920082). C.E.B. was supported in part by a Ruth Kirchstein Fellowship from the National Institute of General Medical Science (F32GM089037). General Medical Sciences and Cancer Institutes Structural Biology Facility at the Advanced Photon Source has been funded in whole or in part with Federal funds from the National Cancer Institute (Y1-CO-1020) and the National Institute of General Medical Sciences (Y1-GM-1104). Use of the Advanced Photon Source was supported by the US Department of Energy, Basic Energy Sciences, Office of Science, under contract no. DE-AC02-06CH11357.",

year = "2013",

month = mar,

doi = "10.1038/nchembio.1159",

language = "الإنجليزيّة",

volume = "9",

pages = "154--156",

journal = "Nature Chemical Biology",

issn = "1552-4450",

publisher = "Nature Research",

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T1 - A conserved asparagine has a structural role in ubiquitin-conjugating enzymes

AU - Berndsen, Christopher E.

AU - Wiener, Reuven

AU - Yu, Ian W.

AU - Ringel, Alison E.

AU - Wolberger, Cynthia

N1 - Funding Information: We thank J. Hurley (National Institute of Diabetes and Digestive and Kidney Diseases) for the Ubc13–Mms2 coexpression plasmid and X. Zhang (Johns Hopkins University) for human E1 protein. We also thank J. Stivers, A. Hengge and L. Spyracopoulos for helpful discussions. This work was supported in part by a grant from the US National Science Foundation (MCB-0920082). C.E.B. was supported in part by a Ruth Kirchstein Fellowship from the National Institute of General Medical Science (F32GM089037). General Medical Sciences and Cancer Institutes Structural Biology Facility at the Advanced Photon Source has been funded in whole or in part with Federal funds from the National Cancer Institute (Y1-CO-1020) and the National Institute of General Medical Sciences (Y1-GM-1104). Use of the Advanced Photon Source was supported by the US Department of Energy, Basic Energy Sciences, Office of Science, under contract no. DE-AC02-06CH11357.

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N2 - 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.

AB - 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.

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U2 - 10.1038/nchembio.1159

DO - 10.1038/nchembio.1159

M3 - مقالة

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SN - 1552-4450

VL - 9

SP - 154

EP - 156

JO - Nature Chemical Biology

JF - Nature Chemical Biology

IS - 3

ER -

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

Abstract

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