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

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.