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DOI | 10.2210/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 | |
| 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: 18242189DOI: 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) |
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