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Structural model of the full-length Ser/Thr protein kinase StkP from S. pneumoniae and its recognition of peptidoglycan fragments
- Source :
- Journal of biomolecular structure & dynamics 36 (2018): 3666–3679. doi:10.1080/07391102.2017.1395767, info:cnr-pdr/source/autori:Righino, Benedetta; Galisson, Frédéric; Pirolli, Davide; Vitale, Serena; Réty, Stéphane; Gouet, Patrice; De Rosa, Maria Cristina/titolo:Structural model of the full-length Ser%2FThr protein kinase StkP from S. pneumoniae and its recognition of peptidoglycan fragments/doi:10.1080%2F07391102.2017.1395767/rivista:Journal of biomolecular structure & dynamics/anno:2018/pagina_da:3666/pagina_a:3679/intervallo_pagine:3666–3679/volume:36, Journal of Biomolecular Structure and Dynamics, Journal of Biomolecular Structure and Dynamics, Taylor & Francis: STM, Behavioural Science and Public Health Titles, 2017, 36 (14), pp.3666-3679. ⟨10.1080/07391102.2017.1395767⟩
- Publication Year :
- 2017
- Publisher :
- Taylor & Francis, 2017.
-
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.
- 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
Subjects
Details
- ISSN :
- 07391102 and 15380254
- Database :
- OpenAIRE
- Journal :
- Journal of biomolecular structure & dynamics 36 (2018): 3666–3679. doi:10.1080/07391102.2017.1395767, info:cnr-pdr/source/autori:Righino, Benedetta; Galisson, Frédéric; Pirolli, Davide; Vitale, Serena; Réty, Stéphane; Gouet, Patrice; De Rosa, Maria Cristina/titolo:Structural model of the full-length Ser%2FThr protein kinase StkP from S. pneumoniae and its recognition of peptidoglycan fragments/doi:10.1080%2F07391102.2017.1395767/rivista:Journal of biomolecular structure & dynamics/anno:2018/pagina_da:3666/pagina_a:3679/intervallo_pagine:3666–3679/volume:36, Journal of Biomolecular Structure and Dynamics, Journal of Biomolecular Structure and Dynamics, Taylor & Francis: STM, Behavioural Science and Public Health Titles, 2017, 36 (14), pp.3666-3679. ⟨10.1080/07391102.2017.1395767⟩
- Accession number :
- edsair.doi.dedup.....af8d8b89be1351bfa8e3e3449e824769
- Full Text :
- https://doi.org/10.6084/m9.figshare.5576512.v1