Substrate-binding destabilizes the hydrophobic cluster to relieve the autoinhibition of bacterial ubiquitin ligase IpaH9.8

Substrate-binding destabilizes the hydrophobic cluster to relieve the autoinhibition of bacterial ubiquitin ligase IpaH9.8

Ye, Xiong et al. present crystal structures of bacterial E3 ubiquitin ligase IpaH9.8 and IpaH9.8LRR–hGBP1. They find that substrate-binding destabilizes the hydrophobic cluster to relieve the autoinhibition of IpaH9.8. This study provides insights into the mechanisms underlying substrate-induced act...

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Main Authors: Yuxin Ye, Yuxian Xiong, Hao Huang
Format: Article
Language:English
Published: Nature Publishing Group 2020-12-01
Series:Communications Biology
Online Access:https://doi.org/10.1038/s42003-020-01492-1
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spelling doaj-a1ceec4815714a919c357f452df6c8882020-12-13T12:22:18ZengNature Publishing GroupCommunications Biology2399-36422020-12-013111410.1038/s42003-020-01492-1Substrate-binding destabilizes the hydrophobic cluster to relieve the autoinhibition of bacterial ubiquitin ligase IpaH9.8Yuxin Ye0Yuxian Xiong1Hao Huang2State Key Laboratory of Chemical Oncogenomics, School of Chemical Biology and Biotechnology, Peking University Shenzhen Graduate SchoolState Key Laboratory of Chemical Oncogenomics, School of Chemical Biology and Biotechnology, Peking University Shenzhen Graduate SchoolState Key Laboratory of Chemical Oncogenomics, School of Chemical Biology and Biotechnology, Peking University Shenzhen Graduate SchoolYe, Xiong et al. present crystal structures of bacterial E3 ubiquitin ligase IpaH9.8 and IpaH9.8LRR–hGBP1. They find that substrate-binding destabilizes the hydrophobic cluster to relieve the autoinhibition of IpaH9.8. This study provides insights into the mechanisms underlying substrate-induced activation of IpaH9.8.https://doi.org/10.1038/s42003-020-01492-1
collection DOAJ
language English
format Article
sources DOAJ
author Yuxin Ye
Yuxian Xiong
Hao Huang
spellingShingle Yuxin Ye
Yuxian Xiong
Hao Huang
Substrate-binding destabilizes the hydrophobic cluster to relieve the autoinhibition of bacterial ubiquitin ligase IpaH9.8
Communications Biology
author_facet Yuxin Ye
Yuxian Xiong
Hao Huang
author_sort Yuxin Ye
title Substrate-binding destabilizes the hydrophobic cluster to relieve the autoinhibition of bacterial ubiquitin ligase IpaH9.8
title_short Substrate-binding destabilizes the hydrophobic cluster to relieve the autoinhibition of bacterial ubiquitin ligase IpaH9.8
title_full Substrate-binding destabilizes the hydrophobic cluster to relieve the autoinhibition of bacterial ubiquitin ligase IpaH9.8
title_fullStr Substrate-binding destabilizes the hydrophobic cluster to relieve the autoinhibition of bacterial ubiquitin ligase IpaH9.8
title_full_unstemmed Substrate-binding destabilizes the hydrophobic cluster to relieve the autoinhibition of bacterial ubiquitin ligase IpaH9.8
title_sort substrate-binding destabilizes the hydrophobic cluster to relieve the autoinhibition of bacterial ubiquitin ligase ipah9.8
publisher Nature Publishing Group
series Communications Biology
issn 2399-3642
publishDate 2020-12-01
description Ye, Xiong et al. present crystal structures of bacterial E3 ubiquitin ligase IpaH9.8 and IpaH9.8LRR–hGBP1. They find that substrate-binding destabilizes the hydrophobic cluster to relieve the autoinhibition of IpaH9.8. This study provides insights into the mechanisms underlying substrate-induced activation of IpaH9.8.
url https://doi.org/10.1038/s42003-020-01492-1
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AT yuxianxiong substratebindingdestabilizesthehydrophobicclustertorelievetheautoinhibitionofbacterialubiquitinligaseipah98
AT haohuang substratebindingdestabilizesthehydrophobicclustertorelievetheautoinhibitionofbacterialubiquitinligaseipah98
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