4MR0

Crystal structure of PfbA, a surface adhesin of Streptococcus pneumoniae

Summary for 4MR0

• Entry DOI: 10.2210/pdb4mr0/pdb
• Descriptor: Plasmin and fibronectin-binding protein A, BETA-MERCAPTOETHANOL, CALCIUM ION, ... (6 entities in total)
• Functional Keywords: surface protein, adhesion, fibronectin, plasminogen, cell adhesion, plasimin and fibronectin-binding protein
• Biological source: Streptococcus pneumoniae
• Cellular location: Secreted, cell wall; Peptidoglycan-anchor (Probable): Q8CYC9
• Total number of polymer chains: 2
• Total formula weight: 143470.24

Authors

Ponnuraj, K.,Beulin, D.S.J. (deposition date: 2013-09-17, release date: 2014-02-05, Last modification date: 2024-03-20)

Primary citation

Beulin, D.S.J.,Yamaguchi, M.,Kawabata, S.,Ponnuraj, K.
Crystal structure of PfbA, a surface adhesin of Streptococcus pneumoniae, provides hints into its interaction with fibronectin
Int.J.Biol.Macromol., 64C:168-173, 2013

PubMed Abstract: 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 1.90Å 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.

PubMed: 24321492
DOI: 10.1016/j.ijbiomac.2013.11.035

Experimental method

X-RAY DIFFRACTION (1.95 Å)