2xzr

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

Structural highlights

2xzr is a 1 chain structure with sequence from Enterobacteria phage P-EibD. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.8Å
Ligands:CL
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

EIBD_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 PubMed

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 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.

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References

  1. ↑ Sandt CH, Hill CW. Four different genes responsible for nonimmune immunoglobulin-binding activities within a single strain of Escherichia coli. Infect Immun. 2000 Apr;68(4):2205-14. PMID:10722621 doi:10.1128/IAI.68.4.2205-2214.2000
  2. ↑ Leo JC, Goldman A. The immunoglobulin-binding Eib proteins from Escherichia coli are receptors for IgG Fc. Mol Immunol. 2009 May;46(8-9):1860-6. PMID:19303642 doi:10.1016/j.molimm.2009.02.024
  3. ↑ Leo JC, Lyskowski A, Hattula K, Hartmann MD, Schwarz H, Butcher SJ, Linke D, Lupas AN, Goldman A. The Structure of E. coli IgG-Binding Protein D Suggests a General Model for Bending and Binding in Trimeric Autotransporter Adhesins. Structure. 2011 Jul 13;19(7):1021-30. PMID:21742268 doi:10.1016/j.str.2011.03.021
  4. ↑ Leo JC, Lyskowski A, Hattula K, Hartmann MD, Schwarz H, Butcher SJ, Linke D, Lupas AN, Goldman A. The Structure of E. coli IgG-Binding Protein D Suggests a General Model for Bending and Binding in Trimeric Autotransporter Adhesins. Structure. 2011 Jul 13;19(7):1021-30. PMID:21742268 doi:10.1016/j.str.2011.03.021

Contents


PDB ID 2xzr

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