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Integrative dynamic structural biology unveils conformers essential for the oligomerization of a large GTPase.
Peulen, Thomas-O; Hengstenberg, Carola S; Biehl, Ralf; Dimura, Mykola; Lorenz, Charlotte; Valeri, Alessandro; Folz, Julian; Hanke, Christian A; Ince, Semra; Vöpel, Tobias; Farago, Bela; Gohlke, Holger; Klare, Johann P; Stadler, Andreas M; Seidel, Claus A M; Herrmann, Christian.
Afiliación
  • Peulen TO; Chair for Molecular Physical Chemistry, Heinrich Heine University Düsseldorf, Düsseldorf, Germany.
  • Hengstenberg CS; Physical Chemistry I, Ruhr University Bochum, Bochum, Germany.
  • Biehl R; Jülich Centre for Neutron Science (JCNS-1) and Institute of Biological Information Processing (IBI-8), Forschungszentrum Jülich GmbH, Jülich, Germany.
  • Dimura M; Chair for Molecular Physical Chemistry, Heinrich Heine University Düsseldorf, Düsseldorf, Germany.
  • Lorenz C; Institut für Pharmazeutische und Medizinische Chemie, Heinrich Heine University Düsseldorf, Düsseldorf, Germany.
  • Valeri A; Jülich Centre for Neutron Science (JCNS-1) and Institute of Biological Information Processing (IBI-8), Forschungszentrum Jülich GmbH, Jülich, Germany.
  • Folz J; Institute of Physical Chemistry, RWTH Aachen University, Düsseldorf, Germany.
  • Hanke CA; Chair for Molecular Physical Chemistry, Heinrich Heine University Düsseldorf, Düsseldorf, Germany.
  • Ince S; Chair for Molecular Physical Chemistry, Heinrich Heine University Düsseldorf, Düsseldorf, Germany.
  • Vöpel T; Chair for Molecular Physical Chemistry, Heinrich Heine University Düsseldorf, Düsseldorf, Germany.
  • Farago B; Physical Chemistry I, Ruhr University Bochum, Bochum, Germany.
  • Gohlke H; Physical Chemistry I, Ruhr University Bochum, Bochum, Germany.
  • Klare JP; Institut Laue-Langevin, Grenoble, France.
  • Stadler AM; Institut für Pharmazeutische und Medizinische Chemie, Heinrich Heine University Düsseldorf, Düsseldorf, Germany.
  • Seidel CAM; Institute of Bio-Geosciences (IBG-4: Bioinformatics), Forschungszentrum Jülich, Jülich, Germany.
  • Herrmann C; Macromolecular Structure Group, Department of Physics, University of Osnabrück, Osnabrück, Germany.
Elife ; 122023 06 14.
Article en En | MEDLINE | ID: mdl-37314846
Guanylate binding proteins (GBPs) are soluble dynamin-like proteins that undergo a conformational transition for GTP-controlled oligomerization and disrupt membranes of intracellular parasites to exert their function as part of the innate immune system of mammalian cells. We apply neutron spin echo, X-ray scattering, fluorescence, and EPR spectroscopy as techniques for integrative dynamic structural biology to study the structural basis and mechanism of conformational transitions in the human GBP1 (hGBP1). We mapped hGBP1's essential dynamics from nanoseconds to milliseconds by motional spectra of sub-domains. We find a GTP-independent flexibility of the C-terminal effector domain in the µs-regime and resolve structures of two distinct conformers essential for an opening of hGBP1 like a pocket knife and for oligomerization. Our results on hGBP1's conformational heterogeneity and dynamics (intrinsic flexibility) deepen our molecular understanding relevant for its reversible oligomerization, GTP-triggered association of the GTPase-domains and assembly-dependent GTP-hydrolysis.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas de Unión al GTP / GTP Fosfohidrolasas Límite: Animals / Humans Idioma: En Revista: Elife Año: 2023 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Reino Unido
Texto completo
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Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas de Unión al GTP / GTP Fosfohidrolasas Límite: Animals / Humans Idioma: En Revista: Elife Año: 2023 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Reino Unido