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- SASDAE6: PsrP functional binding region (Functional binding region (120-39... -
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Open data
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Basic information
Entry | Database: SASBDB / ID: SASDAE6 |
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![]() | PsrP functional binding region
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Function / homology | ![]() Gram-positive-bacterium-type cell wall / symbiont-mediated perturbation of host defense response / single-species biofilm formation / ![]() ![]() ![]() Similarity search - Function |
Biological species | ![]() ![]() ![]() |
![]() | ![]() Title: The BR domain of PsrP interacts with extracellular DNA to promote bacterial aggregation; structural insights into pneumococcal biofilm formation. Authors: Tim Schulte / Cecilia Mikaelsson / Audrey Beaussart / Alexey Kikhney / Maya Deshmukh / Sebastian Wolniak / Anuj Pathak / Christine Ebel / Jonas Löfling / Federico Fogolari / Birgitta ...Authors: Tim Schulte / Cecilia Mikaelsson / Audrey Beaussart / Alexey Kikhney / Maya Deshmukh / Sebastian Wolniak / Anuj Pathak / Christine Ebel / Jonas Löfling / Federico Fogolari / Birgitta Henriques-Normark / Yves F Dufrêne / Dmitri Svergun / Per-Åke Nygren / Adnane Achour / ![]() ![]() ![]() ![]() ![]() 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 ...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. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
-Data source
SASBDB page | ![]() |
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-Related structure data
-Models
Model #563 | ![]() Type: mix / Software: EOM (1.3) / Radius of dummy atoms: 1.90 A / Chi-square value: 2.778889 ![]() |
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Model #564 | ![]() Type: mix / Software: EOM (1.3) / Radius of dummy atoms: 1.90 A / Chi-square value: 2.778889 ![]() |
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Sample
![]() | Name: PsrP functional binding region / Specimen concentration: 0.32-3.00 |
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Buffer | Name: PBS / pH: 7.4 / Comment: Phosphate buffered saline / Composition: Glycerol 5.000 % |
Entity #122 | Name: PsrP BR*(120-395) / Type: protein Description: Functional binding region (120-395) of the pneumococcal serine-rich repeat protein Formula weight: 30.3 / Num. of mol.: 1 / Source: Streptococcus pneumoniae / References: UniProt: A0A0H2URK1 Sequence: HHHHHHSSTV VGSQTAAATE ATAKKVEEDR KKPASDYVAS VTNVNLQSYA KRRKRSVDSI EQLLASIKNA AVFSGNTIVN GAPAINASLN IAKSETKVYT GEGVDSVYRV PIYYKLKVTN DGSKLTFTYT VTYVNPKTND LGNISSMRPG YSIYNSGTST QTMLTLGSDL ...Sequence: HHHHHHSSTV VGSQTAAATE ATAKKVEEDR KKPASDYVAS VTNVNLQSYA KRRKRSVDSI EQLLASIKNA AVFSGNTIVN GAPAINASLN IAKSETKVYT GEGVDSVYRV PIYYKLKVTN DGSKLTFTYT VTYVNPKTND LGNISSMRPG YSIYNSGTST QTMLTLGSDL GKPSGVKNYI TDKNGRQVLS YNTSTMTTQG SGYTWGNGAQ MNGFFAKKGY GLTSSWTVPI TGTDTSFTFT PYAARTDRIG INYFNGGGKV VESSTTSQSL SQSKSLSVSA SQ |
-Experimental information
Beam | Instrument name: ESRF BM29 / City: Grenoble / 国: France ![]() ![]() | |||||||||||||||||||||||||||||||||
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Detector | Name: Pilatus 1M | |||||||||||||||||||||||||||||||||
Scan |
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Distance distribution function P(R) |
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Result |
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