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Structural model of the full-length Ser/Thr protein kinase StkP from S. pneumoniae and its recognition of peptidoglycan fragments.

Authors :
Righino B
Galisson F
Pirolli D
Vitale S
Réty S
Gouet P
De Rosa MC
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.

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