1r17 | pdb_00001r17
Crystal Structure Analysis of S.epidermidis adhesin SdrG binding to Fibrinogen (adhesin-ligand complex)
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| 1r17, resolution 1.86Å | |||||||||||||
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| Ligands: | CA | ||||||||||||
| Gene: | SDRG (Staphylococcus epidermidis) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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. 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 Thu Mar 20 13:45:27 2008
