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ATP-dependent conformational dynamics in a photoactivated adenylate cyclase revealed by fluorescence spectroscopy and small-angle X-ray scattering.
Ujfalusi-Pozsonyi, K; Bódis, E; Nyitrai, M; Kengyel, A; Telek, E; Pécsi, I; Fekete, Z; Varnyuné Kis-Bicskei, N; Mas, C; Moussaoui, D; Pernot, P; Tully, M D; Weik, M; Schirò, G; Kapetanaki, S M; Lukács, A.
Afiliación
  • Ujfalusi-Pozsonyi K; Department of Biophysics, Medical School, University of Pécs, 7624, Pécs, Hungary.
  • Bódis E; Department of Biophysics, Medical School, University of Pécs, 7624, Pécs, Hungary.
  • Nyitrai M; Department of Biophysics, Medical School, University of Pécs, 7624, Pécs, Hungary.
  • Kengyel A; Department of Biophysics, Medical School, University of Pécs, 7624, Pécs, Hungary.
  • Telek E; Department of Biophysics, Medical School, University of Pécs, 7624, Pécs, Hungary.
  • Pécsi I; Department of Biophysics, Medical School, University of Pécs, 7624, Pécs, Hungary.
  • Fekete Z; Department of Biophysics, Medical School, University of Pécs, 7624, Pécs, Hungary.
  • Varnyuné Kis-Bicskei N; Department of Biophysics, Medical School, University of Pécs, 7624, Pécs, Hungary.
  • Mas C; Univ. Grenoble Alpes, CNRS, CEA, EMBL, ISBG, F-38000, Grenoble, France.
  • Moussaoui D; European Synchrotron Radiation Facility (ESRF), Grenoble, France.
  • Pernot P; European Synchrotron Radiation Facility (ESRF), Grenoble, France.
  • Tully MD; European Synchrotron Radiation Facility (ESRF), Grenoble, France.
  • Weik M; Institut de Biologie Structurale (IBS), Université Grenoble Alpes, CEA, CNRS, Grenoble, France.
  • Schirò G; Institut de Biologie Structurale (IBS), Université Grenoble Alpes, CEA, CNRS, Grenoble, France.
  • Kapetanaki SM; Institut de Biologie Structurale (IBS), Université Grenoble Alpes, CEA, CNRS, Grenoble, France. sofia.kapetanaki@aok.pte.hu.
  • Lukács A; Department of Biophysics, Medical School, University of Pécs, 7624, Pécs, Hungary. sofia.kapetanaki@aok.pte.hu.
Commun Biol ; 7(1): 147, 2024 Feb 02.
Article en En | MEDLINE | ID: mdl-38307988
ABSTRACT
Structural insights into the photoactivated adenylate cyclases can be used to develop new ways of controlling cellular cyclic adenosine monophosphate (cAMP) levels for optogenetic and other applications. In this work, we use an integrative approach that combines biophysical and structural biology methods to provide insight on the interaction of adenosine triphosphate (ATP) with the dark-adapted state of the photoactivated adenylate cyclase from the cyanobacterium Oscillatoria acuminata (OaPAC). A moderate affinity of the nucleotide for the enzyme was calculated and the thermodynamic parameters of the interaction have been obtained. Stopped-flow fluorescence spectroscopy and small-angle solution scattering have revealed significant conformational changes in the enzyme, presumably in the adenylate cyclase (AC) domain during the allosteric mechanism of ATP binding to OaPAC with small and large-scale movements observed to the best of our knowledge for the first time in the enzyme in solution upon ATP binding. These results are in line with previously reported drastic conformational changes taking place in several class III AC domains upon nucleotide binding.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Adenosina Trifosfato / Adenilil Ciclasas Idioma: En Revista: Commun Biol Año: 2024 Tipo del documento: Article País de afiliación: Hungria Pais de publicación: Reino Unido
Texto completo
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Imprimir
XML
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Adenosina Trifosfato / Adenilil Ciclasas Idioma: En Revista: Commun Biol Año: 2024 Tipo del documento: Article País de afiliación: Hungria Pais de publicación: Reino Unido