3RFZ

Crystal structure of the FimD usher bound to its cognate FimC:FimH substrate

3RFZ の概要

• エントリーDOI: 10.2210/pdb3rfz/pdb
• 関連するPDBエントリー: 1KLF 1ZE3 2VQI 3BWU 3L48 3OHN
• 分子名称: Type 1 fimbrial adhesin, Outer membrane usher protein, type 1 fimbrial synthesis, Chaperone protein fimC, ... (5 entities in total)
• 機能のキーワード: beta-barrel, pilus assembly, outer-membrane, cell adhesion-transport protein-chaperone complex, cell adhesion-transport-chaperone complex, cell adhesion/transport/chaperone
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Cell outer membrane; Multi-pass membrane protein (By similarity): C6UL88; Periplasm (By similarity): P59590
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 290875.26

構造登録者

Phan, G.,Remaut, H.,Lebedev, A.,Geibel, S.,Waksman, G. (登録日: 2011-04-07, 公開日: 2011-06-01, 最終更新日: 2024-10-30)

主引用文献

Phan, G.,Remaut, H.,Wang, T.,Allen, W.J.,Pirker, K.F.,Lebedev, A.,Henderson, N.S.,Geibel, S.,Volkan, E.,Yan, J.,Kunze, M.B.,Pinkner, J.S.,Ford, B.,Kay, C.W.,Li, H.,Hultgren, S.J.,Thanassi, D.G.,Waksman, G.
Crystal structure of the FimD usher bound to its cognate FimC-FimH substrate.
Nature, 474:49-53, 2011

PubMed Abstract: Type 1 pili are the archetypal representative of a widespread class of adhesive multisubunit fibres in Gram-negative bacteria. During pilus assembly, subunits dock as chaperone-bound complexes to an usher, which catalyses their polymerization and mediates pilus translocation across the outer membrane. Here we report the crystal structure of the full-length FimD usher bound to the FimC-FimH chaperone-adhesin complex and that of the unbound form of the FimD translocation domain. The FimD-FimC-FimH structure shows FimH inserted inside the FimD 24-stranded β-barrel translocation channel. FimC-FimH is held in place through interactions with the two carboxy-terminal periplasmic domains of FimD, a binding mode confirmed in solution by electron paramagnetic resonance spectroscopy. To accommodate FimH, the usher plug domain is displaced from the barrel lumen to the periplasm, concomitant with a marked conformational change in the β-barrel. The amino-terminal domain of FimD is observed in an ideal position to catalyse incorporation of a newly recruited chaperone-subunit complex. The FimD-FimC-FimH structure provides unique insights into the pilus subunit incorporation cycle, and captures the first view of a protein transporter in the act of secreting its cognate substrate.

PubMed: 21637253
DOI: 10.1038/nature10109

実験手法

X-RAY DIFFRACTION (2.8 Å)