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...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2020-12-01
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| Series: | Communications Biology |
| Online Access: | https://doi.org/10.1038/s42003-020-01492-1 |
| _version_ | 1818840852950155264 |
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| author | Yuxin Ye Yuxian Xiong Hao Huang |
| author_facet | Yuxin Ye Yuxian Xiong Hao Huang |
| author_sort | Yuxin Ye |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-12-19T04:16:47Z |
| format | Article |
| id | doaj.art-a1ceec4815714a919c357f452df6c888 |
| institution | Directory Open Access Journal |
| issn | 2399-3642 |
| language | English |
| last_indexed | 2024-12-19T04:16:47Z |
| publishDate | 2020-12-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Communications Biology |
| spelling | doaj.art-a1ceec4815714a919c357f452df6c8882022-12-21T20:36:17ZengNature PortfolioCommunications 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 |
| 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 |
| title | 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_short | 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 |
| url | https://doi.org/10.1038/s42003-020-01492-1 |
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