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1ZE3

Crystal Structure of the Ternary Complex of FIMD (N-Terminal Domain) with FIMC and the Pilin Domain of FIMH

Summary for 1ZE3
Entry DOI10.2210/pdb1ze3/pdb
DescriptorChaperone protein fimC, FimH protein, Outer membrane usher protein fimD, ... (5 entities in total)
Functional Keywordsusher, soluble domain, ternary complex with chaperone and pilus subunit, chaperone-structural-membrane protein complex, chaperone/structural/membrane protein
Biological sourceEscherichia coli
More
Cellular locationPeriplasm: P31697
Fimbrium: P08191
Cell outer membrane; Multi-pass membrane protein (By similarity): P30130
Total number of polymer chains3
Total formula weight49446.69
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 citationNishiyama, 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: 15920478
DOI: 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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数据于2024-10-30公开中

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