1r19

Crystal Structure Analysis of S.epidermidis adhesin SdrG binding to Fibrinogen (Apo structure)

spinqualitylabelsall models 1r19, resolution 3.51Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1r19 is a 4 chain structure with sequence from "albococcus_epidermidis"_winslow_and_winslow_1908 "albococcus epidermidis" winslow and winslow 1908. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1r17 Gene: sdrG ("Albococcus epidermidis" Winslow and Winslow 1908) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [SDRG_STAEP] Binds to the N-terminus of the B beta-chain of human fibrinogen and thereby interferes with thrombin cleavage and release of fibrinopeptide B, thus interfering with fibrin clot formation. This may hinder host defense against microbial infections. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Gram-positive pathogens such as staphylococci contain multiple cell wall-anchored proteins that serve as an interface between the microbe and its environment. Some of these proteins act as adhesins and mediate bacterial attachment to host tissues. SdrG is a cell wall-anchored adhesin from Staphylococcus epidermidis that binds to the Bbeta chain of human fibrinogen (Fg) and is necessary and sufficient for bacterial attachment to Fg-coated biomaterials. Here, we present the crystal structures of the ligand binding region of SdrG as an apoprotein and in complex with a synthetic peptide analogous to its binding site in Fg. Analysis of the crystal structures, along with mutational studies of both the protein and of the peptide, reveals that SdrG binds to its ligand with a dynamic "dock, lock, and latch" mechanism. We propose that this mechanism represents a general mode of ligand binding for structurally related cell wall-anchored proteins of gram-positive bacteria. A "dock, lock, and latch" structural model for a staphylococcal adhesin binding to fibrinogen.,Ponnuraj K, Bowden MG, Davis S, Gurusiddappa S, Moore D, Choe D, Xu Y, Hook M, Narayana SV Cell. 2003 Oct 17;115(2):217-28. PMID:14567919 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Fibrinogen binding protein

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