Academic Journal
Structural Insight into the Role of the PAS Domain for Signal Transduction in Sensor Kinase BvgS
| العنوان: | Structural Insight into the Role of the PAS Domain for Signal Transduction in Sensor Kinase BvgS |
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| المؤلفون: | Dupré, Elian, Clantin, Bernard, Yuan, Youhua, Lecher, Sophie, Lesne, Elodie, Antoine, Rudy, Villeret, Vincent, Jacob-Dubuisson, Françoise |
| المساهمون: | Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 (CIIL), Institut Pasteur de Lille, Pasteur Network (Réseau International des Instituts Pasteur)-Pasteur Network (Réseau International des Instituts Pasteur)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille-Centre Hospitalier Régional Universitaire CHU Lille (CHRU Lille)-Centre National de la Recherche Scientifique (CNRS), Facteurs de Risque et Déterminants Moléculaires des Maladies liées au Vieillissement - U 1167 (RID-AGE), Pasteur Network (Réseau International des Instituts Pasteur)-Pasteur Network (Réseau International des Instituts Pasteur)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille-Centre Hospitalier Régional Universitaire CHU Lille (CHRU Lille) |
| المصدر: | ISSN: 0021-9193. |
| بيانات النشر: | CCSD American Society for Microbiology |
| سنة النشر: | 2021 |
| المجموعة: | LillOA (HAL Lille Open Archive, Université de Lille) |
| مصطلحات موضوعية: | two-component system, Bordetella pertussis, sensor kinases, PAS domain, virulence regulation, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM] |
| الوصف: | International audience ; The two-component system BvgAS controls the virulence regulon in Bordetella pertussis. BvgS is the prototype of a family of sensor histidine kinases harboring periplasmic Venus flytrap (VFT) domains. The VFT domains are connected to the cytoplasmic kinase moiety by helical linkers separated by a Per-ARNT-Sim (PAS) domain. Antagonism between the two linkers, as one forms a coiled coil when the other is dynamic and vice versa, regulates BvgS activity. Here, we solved the structure of the intervening PAS domain by X-ray crystallography. Two forms were obtained that notably differ by the connections between the PAS core domain and the flanking helical linkers. Structure-guided mutagenesis indicated that those connections participate in the regulation of BvgS activity. Thus, the PAS domain appears to function as a switch facilitator module whose conformation determines the output of the system. As many BvgS homologs have similar architectures, the mechanisms unveiled here are likely to generally apply to the regulation of sensor histidine kinases of that family. |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| DOI: | 10.1128/jb.00614-20 |
| الاتاحة: | https://hal.science/hal-03396238 https://hal.science/hal-03396238v1/document https://hal.science/hal-03396238v1/file/Journal%20of%20Bacteriology-2021-Dupr%C3%A9-e00614-20.full.pdf https://doi.org/10.1128/jb.00614-20 |
| Rights: | info:eu-repo/semantics/OpenAccess |
| رقم الانضمام: | edsbas.ED9BD366 |
| قاعدة البيانات: | BASE |
| DOI: | 10.1128/jb.00614-20 |
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