4mbr

3.65 Angstrom Crystal Structure of Serine-rich Repeat Protein (Srr2) from Streptococcus agalactiae

spinqualitylabelsall models 4mbr, resolution 3.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4mbr is a 1 chain structure with sequence from Streptococcus agalactiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q49RA6_STRAG Publication Abstract from PubMed The serine-rich repeat (SRR) glycoproteins of Gram-positive bacteria comprise a large family of cell wall proteins. Streptococcus agalactiae (Group B streptococcus, GBS) expresses either Srr1 or Srr2 on its surface, depending on the strain. Srr1 has recently been shown to bind fibrinogen, and this interaction contributes to the pathogenesis of GBS meningitis. Although strains expressing Srr2 appear to be hypervirulent, no ligand for this adhesin has been described. We now demonstrate that Srr2 also binds human fibrinogen, and that this interaction promotes GBS attachment to endothelial cells. Recombinant Srr1 and Srr2 bound fibrinogen in vitro, with affinities of KD = 2.1 x 10-5 M and 3.7 x 10-6 M, respectively, as measured by surface plasmon resonance spectroscopy. The binding site for Srr1 and Srr2 was localized to tandem repeats 6-8 of the fibrinogen Aalpha chain. The structures of both the Srr1 and Srr2 binding regions were determined and in combination with mutagenesis studies, suggest that both Srr1 and Srr2 interact with a segment of these repeats via a dock, lock, and latch mechanism. Moreover, properties of the latch region may account for the increased affinity between Srr2 and fibrinogen. Together, these studies identify how greater affinity of Srr2 for fibrinogen may contribute to the increased virulence associated with Srr2-expressing strains. Characterization of fibrinogen binding by glycoproteins Srr1 and Srr2 of Streptococcus agalactiae.,Seo HS, Misanov G, Seepersaud R, Doran KS, Dubrovska I, Shuvalova L, Anderson WF, Iverson TM, Sullam PM J Biol Chem. 2013 Oct 28. PMID:24165132 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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