EibD

Crystal structure of an immunoglobulin-binding fragment of the trimeric autotransporter adhesin (TAA) EibD

spinqualitylabelsall models Crystal structure of an immunoglobulin-binding fragment of the trimeric autotransporter adhesin (TAA) EibD (PDB entry 2xqh) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. Structure Features Space Group: H 3 (48.950x48.950x409.600, 90.00x90.00x120.00) Resolution limit: 1.99 Å R/R free: 0.1585/0.1855 Full crystallographic information is available from OCA. Asymmetric unit contains a single polypeptide chain. The biological assembly consists of three copies of the monomer related by a three fold axis. There are five distinct domains: YadA-like β-roll domain; neck domain; right handed coiled-coil domain; mini β-sheet domain; left handed coiled-coil domain; Coild-coil features: cavities chloride coordination by Thr and Asn residues. General information Antibodies: RCSB PDB Molecule of the Month by David Goodsell

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Andrzej Lyskowski, Michal Harel