3ZGH

Crystal structure of the KRT10-binding region domain of the pneumococcal serine rich repeat protein PsrP

Summary for 3ZGH

• Entry DOI: 10.2210/pdb3zgh/pdb
• Related: 3ZGI
• Descriptor: CELL WALL SURFACE ANCHOR FAMILY PROTEIN, ACETATE ION, GLYCEROL, ... (5 entities in total)
• Functional Keywords: structural protein, mscramm, keratin-10
• Biological source: STREPTOCOCCUS PNEUMONIAE
• Total number of polymer chains: 1
• Total formula weight: 22562.81

Authors

Schulte, T.,Loefling, J.,Mikaelsson, C.,Kikhney, A.,Hentrich, K.,Diamante, A.,Ebel, C.,Normark, S.,Svergun, D.,Henriques-Normark, B.,Achour, A. (deposition date: 2012-12-17, release date: 2014-01-08, Last modification date: 2024-05-01)

Primary citation

Schulte, T.,Lofling, J.,Mikaelsson, C.,Kikhney, A.,Hentrich, K.,Diamante, A.,Ebel, C.,Normark, S.,Svergun, D.,Henriques-Normark, B.,Achour, A.
The Basic Keratin 10-Binding Domain of the Virulence-Associated Pneumococcal Serine-Rich Protein Psrp Adopts a Novel Mscramm Fold.
Open Biol., 4:0090-, 2014

PubMed 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.

PubMed: 24430336
DOI: 10.1098/RSOB.130090

Experimental method

X-RAY DIFFRACTION (2 Å)