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The basic keratin 1...
The basic keratin 10-binding domain of the virulence-associated pneumococcal serine-rich protein PsrP adopts a novel MSCRAMM fold
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- Schulte, T (author)
- Karolinska Institutet
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Lofling, J (author)
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Mikaelsson, C (author)
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Kikhney, A (author)
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- Hentrich, K (author)
- Karolinska Institutet
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Diamante, A (author)
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Ebel, C (author)
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- Normark, S (author)
- Karolinska Institutet
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Svergun, D (author)
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- Henriques-Normark, B (author)
- Karolinska Institutet
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- Achour, A (author)
- Karolinska Institutet
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(creator_code:org_t)
- 2014-01
- 2014
- English.
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In: Open biology. - : The Royal Society. - 2046-2441. ; 4:1, s. 130090-
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Abstract
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- Streptococcus pneumoniaeis 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. BR187–385adopts 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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- ref (subject category)
- art (subject category)
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- By the author/editor
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Schulte, T
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Lofling, J
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Mikaelsson, C
-
Kikhney, A
-
Hentrich, K
-
Diamante, A
-
show more...
-
Ebel, C
-
Normark, S
-
Svergun, D
-
Henriques-Normar ...
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Achour, A
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show less...
- Articles in the publication
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Open biology
- By the university
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Karolinska Institutet