The structure of E. coli IgG-binding protein D suggests a general model for bending and binding in trimeric autotransporter adhesins

Leo, JC ORCID: https://orcid.org/0000-0002-7066-7527, Lyskowski, A, Hattula, K, Hartmann, MD, Schwarz, H, Butcher, SJ, Linke, D, Lupas, AN and Goldman, A, 2011. The structure of E. coli IgG-binding protein D suggests a general model for bending and binding in trimeric autotransporter adhesins. Structure, 19 (7), pp. 1021-1030. ISSN 0969-2126

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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.

Item Type:	Journal article
Alternative Title:	Crystal structure of EibD [running title]
Publication Title:	Structure
Creators:	Leo, J.C., Lyskowski, A., Hattula, K., Hartmann, M.D., Schwarz, H., Butcher, S.J., Linke, D., Lupas, A.N. and Goldman, A.
Publisher:	Elsevier
Date:	13 July 2011
Volume:	19
Number:	7
ISSN:	0969-2126
Identifiers:	Number Type 10.1016/j.str.2011.03.021 DOI S0969212611001705 Publisher Item Identifier
Divisions:	Schools > School of Science and Technology
Record created by:	Linda Sullivan
Date Added:	21 Jun 2019 08:22
Last Modified:	25 Jun 2019 13:06
URI:	https://irep.ntu.ac.uk/id/eprint/36885

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