1r17
From Proteopedia
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Crystal Structure Analysis of S.epidermidis adhesin SdrG binding to Fibrinogen (adhesin-ligand complex)
Overview
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.
About this Structure
1R17 is a Single protein structure of sequence from Staphylococcus epidermidis with CA as ligand. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Wed Nov 21 01:11:19 2007
