4mr0 | pdb_00004mr0

Crystal structure of PfbA, a surface adhesin of Streptococcus pneumoniae

spinqualitylabelsall models 4mr0, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4mr0 is a 2 chain structure with sequence from Streptococcus pneumoniae R6. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BME, CA, CL, MN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PFBA_STRR6 Acts as a fibronectin-dependent adhesin and invasin. Binds host (in this case human) fibronectin, plasmin, plasminogen, and human serum albumin. Where the bacteria adhere to human cells there is major recruitment of microvilli which seem to fuse to cover the streptococcal chains. Antibodies to this protein reduce bacterial growth in human blood. Publication Abstract from PubMed PfbA is a surface adhesin and invasin of Streptococcus pneumoniae that binds to human fibronectin and plasminogen of the host extracellular matrix. It is a virulence factor for its pathogenesis. The crystal structure of recombinant PfbA150-607 from S. pneumoniae strain R6, was determined using multiwavelength anomalous dispersion (MAD) method and refined to 1.90A resolution. The structure of rPfbA150-607 revealed that residues Thr150 to Lys570 form a rigid parallel beta helix, followed by a short disordered region (571-607) that consists of beta hairpins. The structural organization of the beta helix resembles that of polysaccharide-modifying enzymes. The structural and sequence features essential for fibronectin-binding observed in the well characterized fibronectin-binding proteins such as FnBPA of Staphylococcus aureus, SfbI of Streptococcus pyogenes and BBK32 of Borrelia burgdorferi has been found in rPfbA150-607. Based on this, it is predicted that the disordered region following the beta helix could be the fibronectin-binding region in PfbA. PfbA150-607 contains relatively high number of surface exposed lysines and these residues are probably involved in binding plasmin(ogen) as observed in other plasminogen-binding proteins. Crystal structure of PfbA, a surface adhesin of Streptococcus pneumoniae, provides hints into its interaction with fibronectin.,Beulin DS, Yamaguchi M, Kawabata S, Ponnuraj K Int J Biol Macromol. 2013 Dec 7;64C:168-173. doi: 10.1016/j.ijbiomac.2013.11.035. PMID:24321492 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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