1ZE3
Crystal Structure of the Ternary Complex of FIMD (N-Terminal Domain) with FIMC and the Pilin Domain of FIMH
Summary for 1ZE3
Entry DOI | 10.2210/pdb1ze3/pdb |
Descriptor | Chaperone protein fimC, FimH protein, Outer membrane usher protein fimD, ... (5 entities in total) |
Functional Keywords | usher, soluble domain, ternary complex with chaperone and pilus subunit, chaperone-structural-membrane protein complex, chaperone/structural/membrane protein |
Biological source | Escherichia coli More |
Cellular location | Periplasm: P31697 Fimbrium: P08191 Cell outer membrane; Multi-pass membrane protein (By similarity): P30130 |
Total number of polymer chains | 3 |
Total formula weight | 49446.69 |
Authors | Nishiyama, M.,Horst, R.,Eidam, O.,Herrmann, T.,Ignatov, O.,Vetsch, M.,Bettendorff, P.,Jelesarov, I.,Grutter, M.G.,Wuthrich, K.,Glockshuber, R.,Capitani, G. (deposition date: 2005-04-17, release date: 2005-06-14, Last modification date: 2023-08-23) |
Primary citation | Nishiyama, M.,Horst, R.,Eidam, O.,Herrmann, T.,Ignatov, O.,Vetsch, M.,Bettendorff, P.,Jelesarov, I.,Glockshuber, R.,Capitani, G. Structural basis of chaperone-subunit complex recognition by the type 1 pilus assembly platform FimD. Embo J., 24:2075-2086, 2005 Cited by PubMed Abstract: Adhesive type 1 pili from uropathogenic Escherichia coli are filamentous protein complexes that are attached to the assembly platform FimD in the outer membrane. During pilus assembly, FimD binds complexes between the chaperone FimC and type 1 pilus subunits in the periplasm and mediates subunit translocation to the cell surface. Here we report nuclear magnetic resonance and X-ray protein structures of the N-terminal substrate recognition domain of FimD (FimD(N)) before and after binding of a chaperone-subunit complex. FimD(N) consists of a flexible N-terminal segment of 24 residues, a structured core with a novel fold, and a C-terminal hinge segment. In the ternary complex, residues 1-24 of FimD(N) specifically interact with both FimC and the subunit, acting as a sensor for loaded FimC molecules. Together with in vivo complementation studies, we show how this mechanism enables recognition and discrimination of different chaperone-subunit complexes by bacterial pilus assembly platforms. PubMed: 15920478DOI: 10.1038/sj.emboj.7600693 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.84 Å) |
Structure validation
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