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...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Yuxin Ye, Yuxian Xiong, Hao Huang
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2020
Materias:
Acceso en línea:https://doaj.org/article/a1ceec4815714a919c357f452df6c888
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
id oai:doaj.org-article:a1ceec4815714a919c357f452df6c888
record_format dspace
spelling oai:doaj.org-article:a1ceec4815714a919c357f452df6c8882021-12-02T16:18:00ZSubstrate-binding destabilizes the hydrophobic cluster to relieve the autoinhibition of bacterial ubiquitin ligase IpaH9.810.1038/s42003-020-01492-12399-3642https://doaj.org/article/a1ceec4815714a919c357f452df6c8882020-12-01T00:00:00Zhttps://doi.org/10.1038/s42003-020-01492-1https://doaj.org/toc/2399-3642Ye, 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.Yuxin YeYuxian XiongHao HuangNature PortfolioarticleBiology (General)QH301-705.5ENCommunications Biology, Vol 3, Iss 1, Pp 1-14 (2020)
institution DOAJ
collection DOAJ
language EN
topic Biology (General)
QH301-705.5
spellingShingle Biology (General)
QH301-705.5
Yuxin Ye
Yuxian Xiong
Hao Huang
Substrate-binding destabilizes the hydrophobic cluster to relieve the autoinhibition of bacterial ubiquitin ligase IpaH9.8
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.
format article
author Yuxin Ye
Yuxian Xiong
Hao Huang
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 Portfolio
publishDate 2020
url https://doaj.org/article/a1ceec4815714a919c357f452df6c888
work_keys_str_mv AT yuxinye substratebindingdestabilizesthehydrophobicclustertorelievetheautoinhibitionofbacterialubiquitinligaseipah98
AT yuxianxiong substratebindingdestabilizesthehydrophobicclustertorelievetheautoinhibitionofbacterialubiquitinligaseipah98
AT haohuang substratebindingdestabilizesthehydrophobicclustertorelievetheautoinhibitionofbacterialubiquitinligaseipah98
_version_ 1718384247461380096