5DFK

Crystal Structure of the Escherichia coli Common Pilus Chaperone, EcpB

5DFK の概要

• エントリーDOI: 10.2210/pdb5dfk/pdb
• 関連するPDBエントリー: 5D6H
• 分子名称: Probable fimbrial chaperone EcpB (2 entities in total)
• 機能のキーワード: chaperone usher, pilus, pili, biofilm, adhesion, biogenesis, e. coli, virulence, structural protein
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24261.31

構造登録者

Garnett, J.A.,Diallo, M.,Matthews, S.J. (登録日: 2015-08-26, 公開日: 2015-11-04, 最終更新日: 2024-11-20)

主引用文献

Pakharukova, N.,Garnett, J.A.,Tuittila, M.,Paavilainen, S.,Diallo, M.,Xu, Y.,Matthews, S.J.,Zavialov, A.V.
Structural Insight into Archaic and Alternative Chaperone-Usher Pathways Reveals a Novel Mechanism of Pilus Biogenesis.
Plos Pathog., 11:e1005269-e1005269, 2015

PubMed Abstract: Gram-negative pathogens express fibrous adhesive organelles that mediate targeting to sites of infection. The major class of these organelles is assembled via the classical, alternative and archaic chaperone-usher pathways. Although non-classical systems share a wider phylogenetic distribution and are associated with a range of diseases, little is known about their assembly mechanisms. Here we report atomic-resolution insight into the structure and biogenesis of Acinetobacter baumannii Csu and Escherichia coli ECP biofilm-mediating pili. We show that the two non-classical systems are structurally related, but their assembly mechanism is strikingly different from the classical assembly pathway. Non-classical chaperones, unlike their classical counterparts, maintain subunits in a substantially disordered conformational state, akin to a molten globule. This is achieved by a unique binding mechanism involving the register-shifted donor strand complementation and a different subunit carboxylate anchor. The subunit lacks the classical pre-folded initiation site for donor strand exchange, suggesting that recognition of its exposed hydrophobic core starts the assembly process and provides fresh inspiration for the design of inhibitors targeting chaperone-usher systems.

PubMed: 26587649
DOI: 10.1371/journal.ppat.1005269

実験手法

X-RAY DIFFRACTION (2.4 Å)