6C53

Cryo-EM structure of the Type 1 pilus rod

6C53 の概要

• エントリーDOI: 10.2210/pdb6c53/pdb
• EMDBエントリー: 7342
• 分子名称: Type-1 fimbrial protein, A chain (1 entity in total)
• 機能のキーワード: type 1 pili, helical rod, adhesive pili, protein fibril
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 11
• 化学式量合計: 174187.67

構造登録者

Zheng, W.,Wang, F.,Luna-Rico, A.,Francetic, O.,Hultgren, S.J.,Egelman, E.H. (登録日: 2018-01-13, 公開日: 2018-01-31, 最終更新日: 2024-10-23)

主引用文献

Spaulding, C.N.,Schreiber, H.L.,Zheng, W.,Dodson, K.W.,Hazen, J.E.,Conover, M.S.,Wang, F.,Svenmarker, P.,Luna-Rico, A.,Francetic, O.,Andersson, M.,Hultgren, S.,Egelman, E.H.
Functional role of the type 1 pilus rod structure in mediating host-pathogen interactions.
Elife, 7:-, 2018

PubMed Abstract: Uropathogenic (UPEC), which cause urinary tract infections (UTI), utilize type 1 pili, a chaperone usher pathway (CUP) pilus, to cause UTI and colonize the gut. The pilus rod, comprised of repeating FimA subunits, provides a structural scaffold for displaying the tip adhesin, FimH. We solved the 4.2 Å resolution structure of the type 1 pilus rod using cryo-electron microscopy. Residues forming the interactive surfaces that determine the mechanical properties of the rod were maintained by selection based on a global alignment of sequences. We identified mutations that did not alter pilus production in vitro but reduced the force required to unwind the rod. UPEC expressing these mutant pili were significantly attenuated in bladder infection and intestinal colonization in mice. This study elucidates an unappreciated functional role for the molecular spring-like property of type 1 pilus rods in host-pathogen interactions and carries important implications for other pilus-mediated diseases.

PubMed: 29345620
DOI: 10.7554/eLife.31662

実験手法

ELECTRON MICROSCOPY (4.2 Å)