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3BWU

Crystal structure of the ternary complex of FimD (N-Terminal Domain, FimDN) with FimC and the N-terminally truncated pilus subunit FimF (FimFt)

3BWU の概要
エントリーDOI10.2210/pdb3bwu/pdb
関連するPDBエントリー1ZE3
分子名称Chaperone protein fimC, Outer membrane usher protein FimD, N-terminal domain, Protein fimF, ... (6 entities in total)
機能のキーワードusher, n-terminal domain, ternary complex with chaperone and pilus subunit, chaperone, structural protein, mebrane protein, structural, membrane protein
由来する生物種Escherichia coli
詳細
細胞内の位置Periplasm: P31697
Cell outer membrane ; Multi- pass membrane protein : P30130
Fimbrium: P08189
タンパク質・核酸の鎖数3
化学式量合計52172.88
構造登録者
Eidam, O.,Grutter, M.G.,Capitani, G. (登録日: 2008-01-10, 公開日: 2008-03-04, 最終更新日: 2024-11-20)
主引用文献Eidam, O.,Dworkowski, F.S.,Glockshuber, R.,Grutter, M.G.,Capitani, G.
Crystal structure of the ternary FimC-FimF(t)-FimD(N) complex indicates conserved pilus chaperone-subunit complex recognition by the usher FimD
Febs Lett., 582:651-655, 2008
Cited by
PubMed Abstract: Type 1 pili, anchored to the outer membrane protein FimD, enable uropathogenic Escherichia coli to attach to host cells. During pilus biogenesis, the N-terminal periplasmic domain of FimD (FimD(N)) binds complexes between the chaperone FimC and pilus subunits via its partly disordered N-terminal segment, as recently shown for the FimC-FimH(P)-FimD(N) ternary complex. We report the structure of a new ternary complex (FimC-FimF(t)-FimD(N)) with the subunit FimF(t) instead of FimH(p). FimD(N) recognizes FimC-FimF(t) and FimC-FimH(P) very similarly, predominantly through hydrophobic interactions. The conserved binding mode at a "hot spot" on the chaperone surface could guide the design of pilus assembly inhibitors.
PubMed: 18242189
DOI: 10.1016/j.febslet.2008.01.030
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.76 Å)
構造検証レポート
Validation report summary of 3bwu
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2026-04-15に公開中

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