Molecular dynamics of the FixJ receiver domain: movement of the beta4-alpha4 loop correlates with the in and out flip of Phe101 - CNRS - Centre national de la recherche scientifique Accéder directement au contenu
Article Dans Une Revue Protein Science Année : 2002

Molecular dynamics of the FixJ receiver domain: movement of the beta4-alpha4 loop correlates with the in and out flip of Phe101

Philippe Roche
  • Fonction : Auteur
Liliane Mouawad
  • Fonction : Auteur
David Perahia
  • Fonction : Auteur
Jean-Pierre Samama
  • Fonction : Auteur

Résumé

FixJ is a two-domain response regulator involved in nitrogen fixation in Sinorhizobium meliloti. Recent X-ray characterization of both the native (unphosphorylated) and the active (phosphorylated) states of the protein identify conformational changes of the beta4-alpha4 loop and the conserved residue Phe101 as the key switches in activation. These structures also allowed investigation of the transition between conformations of this two-component regulatory receiver domain by molecular dynamics simulations. The path for the conformational change was studied with a distance constraint directing the system from one state to the other. The simulations provide evidence for a correlation between the conformation of the beta4-alpha4 loop and the orientation of the residue Phe101. A model presenting the sequence of events during the activation/deactivation process is discussed.

Domaines

Autre [q-bio.OT]

Dates et versions

hal-01213168 , version 1 (07-10-2015)

Identifiants

Citer

Philippe Roche, Liliane Mouawad, David Perahia, Jean-Pierre Samama, Daniel Kahn. Molecular dynamics of the FixJ receiver domain: movement of the beta4-alpha4 loop correlates with the in and out flip of Phe101. Protein Science, 2002, 11 (11), pp.2622-2630. ⟨10.1110/ps.0218802⟩. ⟨hal-01213168⟩

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