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:
Coiled-coil features:
- cavities
- chloride coordination by Thr and Asn residues.
General information
Antibodies: RCSB PDB Molecule of the Month by David Goodsell [1]
