Secondary-structure switch regulates the substrate binding of a YopJ family acetyltransferase
The Yersinia outer protein J (YopJ) family of effectors, which are present in many plant and animal pathogens are non-canonical acetyltransferases that are activated by the eukaryote-specific cofactor inositol hexaphosphate (InsP6). Here, the authors combine X-ray crystallography, biochemical and fu...
| Main Authors: | , , , , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2021-10-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-021-26183-1 |
| _version_ | 1818937201596039168 |
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| author | Yao Xia Rongfeng Zou Maxime Escouboué Liang Zhong Chengjun Zhu Cécile Pouzet Xueqiang Wu Yongjin Wang Guohua Lv Haibo Zhou Pinghua Sun Ke Ding Laurent Deslandes Shuguang Yuan Zhi-Min Zhang |
| author_facet | Yao Xia Rongfeng Zou Maxime Escouboué Liang Zhong Chengjun Zhu Cécile Pouzet Xueqiang Wu Yongjin Wang Guohua Lv Haibo Zhou Pinghua Sun Ke Ding Laurent Deslandes Shuguang Yuan Zhi-Min Zhang |
| author_sort | Yao Xia |
| collection | DOAJ |
| description | The Yersinia outer protein J (YopJ) family of effectors, which are present in many plant and animal pathogens are non-canonical acetyltransferases that are activated by the eukaryote-specific cofactor inositol hexaphosphate (InsP6). Here, the authors combine X-ray crystallography, biochemical and functional analyses to characterise the structure and activation mechanism of the YopJ family effector PopP2 from the plant pathogen Ralstonia solanacearum and observe that InsP6 binding induces major conformational changes in PopP2 with a helix-to-strand fold-switching in its catalytic core. |
| first_indexed | 2024-12-20T05:48:12Z |
| format | Article |
| id | doaj.art-aaf15f09eb474d80af8634f4bdfa1ed2 |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-20T05:48:12Z |
| publishDate | 2021-10-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-aaf15f09eb474d80af8634f4bdfa1ed22022-12-21T19:51:15ZengNature PortfolioNature Communications2041-17232021-10-0112111010.1038/s41467-021-26183-1Secondary-structure switch regulates the substrate binding of a YopJ family acetyltransferaseYao Xia0Rongfeng Zou1Maxime Escouboué2Liang Zhong3Chengjun Zhu4Cécile Pouzet5Xueqiang Wu6Yongjin Wang7Guohua Lv8Haibo Zhou9Pinghua Sun10Ke Ding11Laurent Deslandes12Shuguang Yuan13Zhi-Min Zhang14International Cooperative Laboratory of Traditional Chinese Medicine Modernization and Innovative Drug Development of Chinese Ministry of Education (MOE), College of Pharmacy, Jinan UniversityShenzhen Institutes of Advanced Technology, Chinese Academy of SciencesLaboratoire des Interactions Plantes-Microbes-Environnement (LIPME), INRAE, CNRS, Université de ToulouseInternational Cooperative Laboratory of Traditional Chinese Medicine Modernization and Innovative Drug Development of Chinese Ministry of Education (MOE), College of Pharmacy, Jinan UniversityInternational Cooperative Laboratory of Traditional Chinese Medicine Modernization and Innovative Drug Development of Chinese Ministry of Education (MOE), College of Pharmacy, Jinan UniversityFRAIB-TRI Imaging Platform Facilities, FR AIB, Université de Toulouse, CNRSInstitute for Pharmaceutical Analysis, College of Pharmacy, Jinan UniversityInternational Cooperative Laboratory of Traditional Chinese Medicine Modernization and Innovative Drug Development of Chinese Ministry of Education (MOE), College of Pharmacy, Jinan UniversityDivision of Histology & Embryology, Medical College, Jinan UniversityInstitute for Pharmaceutical Analysis, College of Pharmacy, Jinan UniversityInternational Cooperative Laboratory of Traditional Chinese Medicine Modernization and Innovative Drug Development of Chinese Ministry of Education (MOE), College of Pharmacy, Jinan UniversityInternational Cooperative Laboratory of Traditional Chinese Medicine Modernization and Innovative Drug Development of Chinese Ministry of Education (MOE), College of Pharmacy, Jinan UniversityLaboratoire des Interactions Plantes-Microbes-Environnement (LIPME), INRAE, CNRS, Université de ToulouseShenzhen Institutes of Advanced Technology, Chinese Academy of SciencesInternational Cooperative Laboratory of Traditional Chinese Medicine Modernization and Innovative Drug Development of Chinese Ministry of Education (MOE), College of Pharmacy, Jinan UniversityThe Yersinia outer protein J (YopJ) family of effectors, which are present in many plant and animal pathogens are non-canonical acetyltransferases that are activated by the eukaryote-specific cofactor inositol hexaphosphate (InsP6). Here, the authors combine X-ray crystallography, biochemical and functional analyses to characterise the structure and activation mechanism of the YopJ family effector PopP2 from the plant pathogen Ralstonia solanacearum and observe that InsP6 binding induces major conformational changes in PopP2 with a helix-to-strand fold-switching in its catalytic core.https://doi.org/10.1038/s41467-021-26183-1 |
| spellingShingle | Yao Xia Rongfeng Zou Maxime Escouboué Liang Zhong Chengjun Zhu Cécile Pouzet Xueqiang Wu Yongjin Wang Guohua Lv Haibo Zhou Pinghua Sun Ke Ding Laurent Deslandes Shuguang Yuan Zhi-Min Zhang Secondary-structure switch regulates the substrate binding of a YopJ family acetyltransferase Nature Communications |
| title | Secondary-structure switch regulates the substrate binding of a YopJ family acetyltransferase |
| title_full | Secondary-structure switch regulates the substrate binding of a YopJ family acetyltransferase |
| title_fullStr | Secondary-structure switch regulates the substrate binding of a YopJ family acetyltransferase |
| title_full_unstemmed | Secondary-structure switch regulates the substrate binding of a YopJ family acetyltransferase |
| title_short | Secondary-structure switch regulates the substrate binding of a YopJ family acetyltransferase |
| title_sort | secondary structure switch regulates the substrate binding of a yopj family acetyltransferase |
| url | https://doi.org/10.1038/s41467-021-26183-1 |
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