6FJY

Crystal structure of CsuC-CsuE chaperone-tip adhesion subunit pre-assembly complex from archaic chaperone-usher Csu pili of Acinetobacter baumannii

6FJY の概要

• エントリーDOI: 10.2210/pdb6fjy/pdb
• 分子名称: CsuC, Protein CsuE, ... (4 entities in total)
• 機能のキーワード: ig-like fold, beta sandwich, donor-strand complementation, cell adhesion
• 由来する生物種: Acinetobacter baumannii; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 122943.78

構造登録者

Pakharukova, N.A.,Tuitilla, M.,Paavilainen, S.,Zavialov, A.V. (登録日: 2018-01-23, 公開日: 2018-05-16, 最終更新日: 2025-04-09)

主引用文献

Pakharukova, N.,Tuittila, M.,Paavilainen, S.,Malmi, H.,Parilova, O.,Teneberg, S.,Knight, S.D.,Zavialov, A.V.
Structural basis forAcinetobacter baumanniibiofilm formation.
Proc. Natl. Acad. Sci. U.S.A., 115:5558-5563, 2018

PubMed Abstract: -a leading cause of nosocomial infections-has a remarkable capacity to persist in hospital environments and medical devices due to its ability to form biofilms. Biofilm formation is mediated by Csu pili, assembled via the "archaic" chaperone-usher pathway. The X-ray structure of the CsuC-CsuE chaperone-adhesin preassembly complex reveals the basis for bacterial attachment to abiotic surfaces. CsuE exposes three hydrophobic finger-like loops at the tip of the pilus. Decreasing the hydrophobicity of these abolishes bacterial attachment, suggesting that archaic pili use tip-fingers to detect and bind to hydrophobic cavities in substrates. Antitip antibody completely blocks biofilm formation, presenting a means to prevent the spread of the pathogen. The use of hydrophilic materials instead of hydrophobic plastics in medical devices may represent another simple and cheap solution to reduce pathogen spread. Phylogenetic analysis suggests that the tip-fingers binding mechanism is shared by all archaic pili carrying two-domain adhesins. The use of flexible fingers instead of classical receptor-binding cavities is presumably more advantageous for attachment to structurally variable substrates, such as abiotic surfaces.

PubMed: 29735695
DOI: 10.1073/pnas.1800961115

実験手法

X-RAY DIFFRACTION (2.31 Å)