5dza

Streptococcus agalactiae AgI/II polypeptide BspA C terminal domain (WT)

spinqualitylabelsall models 5dza, resolution 2.19Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5dza is a 1 chain structure with sequence from Streptococcus agalactiae NEM316. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.19Å Ligands: EDO, PEG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Streptococcus agalactiae (Group B Streptococcus, GBS) is the predominant cause of early-onset infectious disease in neonates and is responsible for life threatening infections in elderly and immune-compromised individuals. Clinical manifestations of GBS infection include sepsis, pneumonia and meningitis. Here we describe BspA, a deviant antigen I/II family polypeptide that confers adhesive properties linked to pathogenesis in GBS. Heterologous expression of BspA on the surface of the non-adherent bacterium Lactococcus lactis confers adherence to scavenger receptor gp340, human vaginal epithelium, and to the fungus Candida albicans Complementary crystallographic and biophysical characterization of BspA reveal a novel beta-sandwich adhesion domain and unique asparagine-dependent super-helical stalk. Collectively these findings establish a new bacterial adhesin structure that has in effect been hijacked by a pathogenic Streptococcus species to provide competitive advantage in human mucosal infections. Structural and Functional Analysis of Cell Wall-Anchored Polypeptide Adhesin BspA in Streptococcus agalactiae.,Rego S, Heal TJ, Pidwill GR, Till M, Robson A, Lamont RJ, Sessions RB, Jenkinson HF, Race PR, Nobbs AH J Biol Chem. 2016 Jun 15. pii: jbc.M116.726562. PMID:27311712 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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