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From Proteopedia
Escherichia coli Immunoglobulin-binding protein EibD 391-438 FUSED TO GCN4 ADAPTORS
Structural highlights
FunctionEIBD_ECOLX Binds (in a non-immune fashion) to the Fc portion of human IgA and IgG; binding occurs on the cell surface. Confers the ability to survive exposure to human serum exposure (PubMed:10722621). Binds to the Fc portion of human IgG, IgA and to whole mouse antibodies also via Fc (PubMed:19303642). Upon overexpression cells acquire an extra cell surface layer that forms a zipper-like contact between cells; cells autoagglutinate and form biofilm more readily, suggesting it may play a role in defense against a host (PubMed:21742268).[1] [2] [3] Publication Abstract from PubMedThe Escherichia coli Ig-binding (Eib) proteins are trimeric autotransporter adhesins (TAAs) and receptors for IgG Fc. We present the structure of a large fragment of the passenger domain of EibD, the first TAA structure to have both a YadA-like head domain and the entire coiled-coil stalk. The stalk begins as a right-handed superhelix, but switches handedness halfway down. An unexpected beta-minidomain joins the two and inserts a approximately 120 degrees rotation such that there is no net twist between the beginning and end of the stalk. This may be important in folding and autotransport. The surprisingly large cavities we found in EibD and other TAAs may explain how TAAs bend to bind their ligands. We identified how IgA and IgG bind and modeled the EibD-IgG Fc complex. We further show that EibD promotes autoagglutination and biofilm formation and forms a fibrillar layer covering the cell surface making zipper-like contacts between cells. The Structure of E. coli IgG-Binding Protein D Suggests a General Model for Bending and Binding in Trimeric Autotransporter Adhesins.,Leo JC, Lyskowski A, Hattula K, Hartmann MD, Schwarz H, Butcher SJ, Linke D, Lupas AN, Goldman A Structure. 2011 Jul 13;19(7):1021-30. PMID:21742268[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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