2XZR

Escherichia coli Immunoglobulin-binding protein EibD 391-438 FUSED TO GCN4 ADAPTORS

Summary for 2XZR

• Entry DOI: 10.2210/pdb2xzr/pdb
• Related: 2XQH
• Descriptor: IMMUNOGLOBULIN-BINDING PROTEIN EIBD, CHLORIDE ION (3 entities in total)
• Functional Keywords: cell adhesion, trimeric autotransporter adhesin, taa, protein export
• Biological source: ENTEROBACTERIA PHAGE P-EIBD
• Total number of polymer chains: 1
• Total formula weight: 13694.41

Authors

Hartmann, M.D.,Hernandez Alvarez, B.,Ridderbusch, O.,Deiss, S.,Lupas, A.N. (deposition date: 2010-11-28, release date: 2011-07-20, Last modification date: 2023-12-20)

Primary citation

Leo, J.C.,Lyskowski, A.,Hattula, K.,Hartmann, M.D.,Schwarz, H.,Butcher, S.J.,Linke, D.,Lupas, A.N.,Goldman, A.
The Structure of E. Coli Igg-Binding Protein D Suggests a General Model for Bending and Binding in Trimeric Autotransporter Adhesins.
Structure, 19:1021-, 2011

PubMed Abstract: The 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 β-minidomain joins the two and inserts a ∼120° 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.

PubMed: 21742268
DOI: 10.1016/J.STR.2011.03.021

Experimental method

X-RAY DIFFRACTION (2.8 Å)