5JUI

domain-swapped dimer of the the KRT10-binding region (BR) of PsrP

Summary for 5JUI

• Entry DOI: 10.2210/pdb5jui/pdb
• Related: 3ZGH
• Descriptor: Cell wall surface anchor family protein, SODIUM ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: streptococcus pneumoniae, pneumococcal serine rich repeat protein, oligomerisation, bacterial aggregation, biofilm formation, dna, structural protein
• Biological source: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
• Total number of polymer chains: 3
• Total formula weight: 64338.07

Authors

Schulte, T.,Mikaelsson, C.,Achour, A. (deposition date: 2016-05-10, release date: 2017-03-15, Last modification date: 2024-01-10)

Primary citation

Schulte, T.,Mikaelsson, C.,Beaussart, A.,Kikhney, A.,Deshmukh, M.,Wolniak, S.,Pathak, A.,Ebel, C.,Lofling, J.,Fogolari, F.,Henriques-Normark, B.,Dufrene, Y.F.,Svergun, D.,Nygren, P.A.,Achour, A.
The BR domain of PsrP interacts with extracellular DNA to promote bacterial aggregation; structural insights into pneumococcal biofilm formation.
Sci Rep, 6:32371-32371, 2016

PubMed Abstract: The major human pathogen Streptococcus pneumoniae is a leading cause of disease and death worldwide. Pneumococcal biofilm formation within the nasopharynx leads to long-term colonization and persistence within the host. We have previously demonstrated that the capsular surface-associated pneumococcal serine rich repeat protein (PsrP), key factor for biofilm formation, binds to keratin-10 (KRT10) through its microbial surface component recognizing adhesive matrix molecule (MSCRAMM)-related globular binding region domain (BR187-385). Here, we show that BR187-385 also binds to DNA, as demonstrated by electrophoretic mobility shift assays and size exclusion chromatography. Further, heterologous expression of BR187-378 or the longer BR120-378 construct on the surface of a Gram-positive model host bacterium resulted in the formation of cellular aggregates that was significantly enhanced in the presence of DNA. Crystal structure analyses revealed the formation of BR187-385 homo-dimers via an intermolecular β-sheet, resulting in a positively charged concave surface, shaped to accommodate the acidic helical DNA structure. Furthermore, small angle X-ray scattering and circular dichroism studies indicate that the aggregate-enhancing N-terminal region of BR120-166 adopts an extended, non-globular structure. Altogether, our results suggest that PsrP adheres to extracellular DNA in the biofilm matrix and thus promotes pneumococcal biofilm formation.

PubMed: 27582320
DOI: 10.1038/srep32371

Experimental method

X-RAY DIFFRACTION (2.1 Å)