Back to Search
Start Over
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 [J Biomol Struct Dyn] 2018 Nov; Vol. 36 (14), pp. 3666-3679. Date of Electronic Publication: 2017 Nov 07. - Publication Year :
- 2018
-
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 :
- Amino Acid Sequence
Molecular Conformation
Molecular Docking Simulation
Molecular Dynamics Simulation
Protein Binding
Protein Interaction Domains and Motifs
Recombinant Proteins
Structure-Activity Relationship
Bacterial Proteins chemistry
Models, Molecular
Peptidoglycan chemistry
Protein Serine-Threonine Kinases chemistry
Streptococcus pneumoniae enzymology
Subjects
Details
- Language :
- English
- ISSN :
- 1538-0254
- Volume :
- 36
- Issue :
- 14
- Database :
- MEDLINE
- Journal :
- Journal of biomolecular structure & dynamics
- Publication Type :
- Academic Journal
- Accession number :
- 29057709
- Full Text :
- https://doi.org/10.1080/07391102.2017.1395767