The basic keratin 10-binding domain of the virulence-associated pneumococcal serine-rich protein PsrP adopts a novel MSCRAMM fold.

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.
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Article dans une revue
Open Biology, Royal Society, 2013, 4, pp.130090
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http://hal.univ-grenoble-alpes.fr/hal-01130606
Contributeur : Frank Thomas <>
Soumis le : jeudi 12 mars 2015 - 09:34:13
Dernière modification le : jeudi 11 janvier 2018 - 06:26:29

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Tim Schulte, Jonas Löfling, Cecilia Mikaelsson, Alexey Kikhney, Karina Hentrich, et al.. The basic keratin 10-binding domain of the virulence-associated pneumococcal serine-rich protein PsrP adopts a novel MSCRAMM fold.. Open Biology, Royal Society, 2013, 4, pp.130090. 〈hal-01130606〉

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