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- SASDAR3: PsrP functional binding region (Functional binding region (187-38... -
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Open data
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Basic information
Entry | Database: SASBDB / ID: SASDAR3 |
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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 / cell adhesion / cell surface / DNA binding / extracellular region Similarity search - Function |
Biological species | ![]() ![]() |
![]() | ![]() 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 ...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. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
-Models
Model #180 | ![]() Type: mix / Software: EOM (1.3) / Radius of dummy atoms: 1.90 A / Chi-square value: 0.582169 ![]() |
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Model #181 | ![]() Type: mix / Software: EOM (1.3) / Radius of dummy atoms: 1.90 A / Chi-square value: 0.582169 ![]() |
Model #182 | ![]() Type: mix / Software: EOM (1.3) / Radius of dummy atoms: 1.90 A / Chi-square value: 0.582169 ![]() |
Model #183 | ![]() Type: mix / Software: EOM (1.3) / Radius of dummy atoms: 1.90 A / Chi-square value: 0.582169 ![]() |
Model #184 | ![]() Type: mix / Software: EOM (1.3) / Radius of dummy atoms: 1.90 A / Chi-square value: 0.582169 ![]() |
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Sample
![]() | Name: PsrP functional binding region / Specimen concentration: 1.10-8.70 |
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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 ...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: ![]() ![]() ![]() | ||||||||||||||||||
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Detector | Name: Pilatus 1M-W / Pixsize x: 0.172 mm | ||||||||||||||||||
Scan |
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Distance distribution function P(R) |
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Result |
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