Item request has been placed! ×
Item request cannot be made. ×
loading  Processing Request

Mechanism of transmembrane signaling by sensor histidine kinases

Item request has been placed! ×
Item request cannot be made. ×
loading   Processing Request
اقرأ أكثر حفظ في قائمتي
  • معلومة اضافية
    • Contributors:
      Moscow Institute of Physics and Technology Moscow (MIPT); Institute of Complex Systems (ICS); Forschungszentrum Jülich GmbH; Helmholtz-Gemeinschaft = Helmholtz Association-Helmholtz-Gemeinschaft = Helmholtz Association; Institut de biologie structurale (IBS - UMR 5075 ); Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes 2016-2019 (UGA 2016-2019 )-Institut de Recherche Interdisciplinaire de Grenoble (IRIG); Direction de Recherche Fondamentale (CEA) (DRF (CEA)); Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)); Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA); European Synchrotron Radiation Facility (ESRF); Institute of Crystallography Aachen; Rheinisch-Westfälische Technische Hochschule Aachen University (RWTH); European Molecular Biology Laboratory Hamburg (EMBL); Algorithms for Modeling and Simulation of Nanosystems (NANO-D); Inria Grenoble - Rhône-Alpes; Institut National de Recherche en Informatique et en Automatique (Inria)-Institut National de Recherche en Informatique et en Automatique (Inria)-Institut polytechnique de Grenoble - Grenoble Institute of Technology (Grenoble INP )-Laboratoire Jean Kuntzmann (LJK ); Institut polytechnique de Grenoble - Grenoble Institute of Technology (Grenoble INP )-Institut National de Recherche en Informatique et en Automatique (Inria)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes 2016-2019 (UGA 2016-2019 )-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes 2016-2019 (UGA 2016-2019 ); Institut für Physikalische Biologie Düsseldorfd; Heinrich Heine Universität Düsseldorf = Heinrich Heine University Düsseldorf; ANR-10-INBS-0005,FRISBI,Infrastructure Française pour la Biologie Structurale Intégrée(2010)
    • بيانات النشر:
      HAL CCSD
      American Association for the Advancement of Science (AAAS)
    • الموضوع:
      2017
    • Collection:
      Université Grenoble Alpes: HAL
    • نبذة مختصرة :
      International audience ; One of the major and essential classes of transmembrane (TM) receptors, present in all domains of life, is sensor histidine kinases (HKs), parts of two-component signaling systems (TCS). The structural mechanisms of transmembrane signaling by these sensors are poorly understood. We present here crystal structures of the periplasmic sensor domain, the TM domain and the cytoplasmic HAMP domain of the Escherichia coli nitrate/nitrite sensor HK NarQ in the ligand-bound and mutated ligand-free states. The structures reveal that the ligand binding induces significant rearrangements and piston-like shifts of TM helices. The HAMP domain protomers undergo lever-like motions and convert the piston-like motions into helical rotations. Our findings provide the structural framework for complete understanding of TM TCS signaling and for development of antimicrobial treatments targeting TCS.
    • Relation:
      hal-01526454; https://hal.science/hal-01526454; https://hal.science/hal-01526454/document; https://hal.science/hal-01526454/file/NarQ-Author-Version.pdf
    • الرقم المعرف:
      10.1126/science.aah6345
    • Rights:
      http://hal.archives-ouvertes.fr/licences/copyright/ ; info:eu-repo/semantics/OpenAccess
    • الرقم المعرف:
      edsbas.4CF102A7