1. Structural model of the full-length Ser/Thr protein kinase StkP from S. pneumoniae and its recognition of peptidoglycan fragments
- Author
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Frédéric Galisson, Maria Cristina De Rosa, Serena Vitale, Davide Pirolli, Patrice Gouet, Stéphane Réty, Benedetta Righino, Laboratoire Epigenetique et Cancer, Centre National de la Recherche Scientifique (CNRS), Laboratoire de Biologie et de Pharmacologie Appliquée (LBPA), École normale supérieure - Cachan (ENS Cachan)-Centre National de la Recherche Scientifique (CNRS), Microbiologie moléculaire et biochimie structurale / Molecular Microbiology and Structural Biochemistry (MMSB), Université Claude Bernard Lyon 1 (UCBL), and Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS)
- Subjects
penicillin-binding protein and serine/threonine kinase associated ,SAXS ,StkP ,eSTKs ,Models, Molecular ,0301 basic medicine ,Cell division ,[SDV]Life Sciences [q-bio] ,030106 microbiology ,Molecular Conformation ,Peptidoglycan ,Molecular Dynamics Simulation ,Protein Serine-Threonine Kinases ,Biology ,Structure-Activity Relationship ,03 medical and health sciences ,chemistry.chemical_compound ,Bacterial Proteins ,Structural Biology ,[SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology ,Protein Interaction Domains and Motifs ,Amino Acid Sequence ,eukaryotic-like serine/threonine protein kinases ,modeling ,molecular dynamics ,muropeptide docking ,Protein kinase A ,Molecular Biology ,ComputingMilieux_MISCELLANEOUS ,ASTA domain ,PASTA ,[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM] ,General Medicine ,Recombinant Proteins ,PASTA domain ,Cell biology ,Molecular Docking Simulation ,Transmembrane domain ,Streptococcus pneumoniae ,030104 developmental biology ,Protein kinase domain ,chemistry ,Biochemistry ,Docking (molecular) ,Intracellular ,Protein Binding - Abstract
The unique eukaryotic-like Ser/Thr protein kinases of Streptococcus pneumoniae, StkP, plays a primary role in the cell division process. It is composed of an intracellular kinase domain, a transmembrane helix and four extracellular PASTA subunits. PASTA domains were shown to interact with cell wall fragments but the key questions related to the molecular mechanism governing ligand recognition remain unclear. To address this issue, the full-length structural model of StkP was generated by combining small-angle X-ray scattering data with the results of computer simulations. Docking and molecular dynamics studies on the generated three-dimensional model structure reveal the possibility of peptidoglycan fragment binding at the hinge regions between PASTA subunits with a preference for a bent hinge between PASTA3 and PASTA4.
- Published
- 2017
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