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1ZE3

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

1ZE3 の概要
エントリーDOI10.2210/pdb1ze3/pdb
分子名称Chaperone protein fimC, FimH protein, Outer membrane usher protein fimD, ... (5 entities in total)
機能のキーワードusher, soluble domain, ternary complex with chaperone and pilus subunit, chaperone-structural-membrane protein complex, chaperone/structural/membrane protein
由来する生物種Escherichia coli
詳細
細胞内の位置Periplasm: P31697
Fimbrium: P08191
Cell outer membrane; Multi-pass membrane protein (By similarity): P30130
タンパク質・核酸の鎖数3
化学式量合計49446.69
構造登録者
主引用文献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: 15920478
DOI: 10.1038/sj.emboj.7600693
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.84 Å)
構造検証レポート
Validation report summary of 1ze3
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-12-31に公開中

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