1ZDX

Solution Structure of the type 1 pilus assembly platform FimD(25-125)

1ZDX の概要

• エントリーDOI: 10.2210/pdb1zdx/pdb
• 関連するPDBエントリー: 1ZDV
• NMR情報: BMRB: 6779
• 分子名称: Outer membrane usher protein fimD (1 entity in total)
• 機能のキーワード: beta sheet, alpha helix, membrane protein
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell outer membrane; Multi-pass membrane protein (By similarity): P30130
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10866.24

構造登録者

Nishiyama, M.,Horst, R.,Herrmann, T.,Vetsch, M.,Bettendorff, P.,Ignatov, O.,Grutter, M.,Wuthrich, K.,Glockshuber, R.,Capitani, G. (登録日: 2005-04-15, 公開日: 2005-06-14, 最終更新日: 2024-05-22)

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

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

実験手法

SOLUTION NMR