SASDAR3: PsrP functional binding region (Functional binding region (187-38...

Basic information

• Entry: Database: SASBDB / ID: SASDAR3

Sample

PsrP functional binding region

• Functional binding region (187-385) of the pneumococcal serine-rich repeat protein (protein), PsrP BR(187-385), Streptococcus pneumoniae

Function / homology

Function:

Gram-positive-bacterium-type cell wall / symbiont-mediated perturbation of host defense response / single-species biofilm formation / cell adhesion / cell surface / DNA binding / extracellular region

Domain/homology:

Serine-rich repeat adhesion glycoprotein / : / LPXTG cell wall anchor motif / Gram-positive cocci surface proteins LPxTG motif profile. / LPXTG cell wall anchor domain

Component:

Pneumococcal serine-rich repeat protein

• Biological species: Streptococcus pneumoniae (bacteria)
• Citation: Journal: Open Biol / Year: 2014; Title: The basic keratin 10-binding domain of the virulence-associated pneumococcal serine-rich protein PsrP adopts a novel MSCRAMM fold.; Authors: Tim Schulte / Jonas Löfling / Cecilia Mikaelsson / Alexey Kikhney / Karina Hentrich / Aurora Diamante / Christine Ebel / Staffan Normark / Dmitri Svergun / Birgitta Henriques-Normark / Adnane Achour / ; Abstract: Streptococcus pneumoniae is a major human pathogen, and a leading cause of disease and death worldwide. Pneumococcal invasive disease is triggered by initial asymptomatic colonization of the human upper respiratory tract. The pneumococcal serine-rich repeat protein (PsrP) is a lung-specific virulence factor whose functional binding region (BR) binds to keratin-10 (KRT10) and promotes pneumococcal biofilm formation through self-oligomerization. We present the crystal structure of the KRT10-binding domain of PsrP (BR187-385) determined to 2.0 Å resolution. BR187-385 adopts a novel variant of the DEv-IgG fold, typical for microbial surface components recognizing adhesive matrix molecules adhesins, despite very low sequence identity. An extended β-sheet on one side of the compressed, two-sided barrel presents a basic groove that possibly binds to the acidic helical rod domain of KRT10. Our study also demonstrates the importance of the other side of the barrel, formed by extensive well-ordered loops and stabilized by short β-strands, for interaction with KRT10.

Contact author

• Al Kikhney (EMBL-Hamburg, European Molecular Biology Laboratory (EMBL) - Hamburg outstation, Notkestraße 85, Geb. 25A, 22607 Hamburg, Deutschland, Germany)

Models

• Model #180: ; Type: mix / Software: EOM (1.3) / Radius of dummy atoms: 1.90 A / Chi-square value: 0.582169; Search similar-shape structures of this assembly by Omokage search (details)
• Model #181: ; Type: mix / Software: EOM (1.3) / Radius of dummy atoms: 1.90 A / Chi-square value: 0.582169; Search similar-shape structures of this assembly by Omokage search (details)
• Model #182: ; Type: mix / Software: EOM (1.3) / Radius of dummy atoms: 1.90 A / Chi-square value: 0.582169; Search similar-shape structures of this assembly by Omokage search (details)
• Model #183: ; Type: mix / Software: EOM (1.3) / Radius of dummy atoms: 1.90 A / Chi-square value: 0.582169; Search similar-shape structures of this assembly by Omokage search (details)
• Model #184: ; Type: mix / Software: EOM (1.3) / Radius of dummy atoms: 1.90 A / Chi-square value: 0.582169; Search similar-shape structures of this assembly by Omokage search (details)

Sample

• Sample: Name: PsrP functional binding region / Specimen concentration: 1.10-8.70
• Buffer: Name: sodium citrate / Concentration: 20.00 mM / pH: 5.5 / Comment: buffer for BR(187-385) / Composition: NaCl 250.000 mM, glycerol 2.500 %

Entity #37

Name: PsrP BR(187-385) / Type: protein
Description: Functional binding region (187-385) of the pneumococcal serine-rich repeat protein
Formula weight: 22.12 / Num. of mol.: 1 / Source: Streptococcus pneumoniae / References: UniProt: A0A0H2URK1
Sequence:

HHHHHHSGNT IVNGAPAINA SLNIAKSETK VYTGEGVDSV YRVPIYYKLK VTNDGSKLTF TYTVTYVNPK TNDLGNISSM RPGYSIYNSG TSTQTMLTLG SDLGKPSGVK NYITDKNGRQ VLSYNTSTMT TQGSGYTWGN GAQMNGFFAK KGYGLTSSWT VPITGTDTSF TFTPYAARTD RIGINYFNGG GKVVESSTTS QSLSQ

Experimental information

• Beam: Instrument name: DORIS III X33 / City: Hamburg / 国: Germany / Shape: 0.6 / Type of source: X-ray synchrotron / Wavelength: 0.15 Å / Dist. spec. to detc.: 2.7 mm
• Detector: Name: Pilatus 1M-W / Pixsize x: 0.172 mm

Scan

Title: PsrP functional binding region / Measurement date: Jul 2, 2011 / Storage temperature: 10 °C / Cell temperature: 10 °C / Exposure time: 15 sec. / Number of frames: 8 / Unit: 1/nm /

	Min	Max
Q	0.1984	6.0214

Distance distribution function P(R)

Sofotware P(R): GNOM 4.5a / Number of points: 404 /

	Min	Max
Q	0.2476	3.554
P(R) point	18	421
R	0	7.706

Result

D max: 7.7 / Type of curve: merged / Standard: BSA /

	Experimental	Porod
MW	18 kDa	23 kDa
Volume	-	37 nm3

	P(R)	Guinier
Forward scattering, I0	16.34	16.7
Radius of gyration, Rg	2.25 nm	2.27 nm