|3asw, resolution 2.60Å ()|
|Gene:||clfB, SA2423 (Staphylococcus aureus)|
Structural and biochemical characterization of ClfB:ligand interactions
Clumping factor B (ClfB) from Staphylococcus aureus is a bifunctional protein that binds to human cytokeratin 10 (K10) and fibrinogen (Fg). ClfB has been implicated in S. aureus colonization of nasal epithelium and is therefore a key virulence factor. People colonized with S. aureus are at an increased risk for invasive staphylococcal disease. In this study, we have determined the crystal structures of the ligand-binding region of ClfB in an apo-form and in complex with human K10 and Fg alpha-chain-derived peptides, respectively. We have determined the structures of MSCRAMM binding to two ligands with different sequences in the same site showing the versatile nature of the ligand recognition mode of microbial surface components recognizing adhesive matrix molecules. Both ligands bind ClfB by parallel beta-sheet complementation as observed for the clumping factor A.gamma-chain peptide complex. The beta-sheet complementation is shorter in the ClfB.Fg alpha-chain peptide complex. The structures show that several residues in ClfB are important for binding to both ligands, whereas others only make contact with one of the ligands. A common motif GSSGXG found in both ligands is part of the ClfB-binding site. This motif is found in many human proteins thus raising the possibility that ClfB recognizes additional ligands.
Structural and biochemical characterization of Staphylococcus aureus clumping factor B/ligand interactions., Ganesh VK, Barbu EM, Deivanayagam CC, Le B, Anderson AS, Matsuka YV, Lin SL, Foster TJ, Narayana SV, Hook M, J Biol Chem. 2011 Jul 22;286(29):25963-72. Epub 2011 May 3. PMID:021543319
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.