3QS2

Crystal structure of the biofilm forming subunit of the E. coli common pilus: full length domain swapped dimer of EcpA

3QS2 の概要

• エントリーDOI: 10.2210/pdb3qs2/pdb
• 関連するPDBエントリー: 3QS3
• 分子名称: Fimbrillin matB homolog, IODIDE ION (3 entities in total)
• 機能のキーワード: pilin, ig-like fold, biofilms, adhesion, immunoglobulin-like fold, major pilin domain involved in biofilms, intermolecular and hydrophobic abiotic surface binding, extracellular membrane, cell adhesion
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 42150.03

構造登録者

Garnett, J.A.,Matthews, S.J. (登録日: 2011-02-19, 公開日: 2012-02-22, 最終更新日: 2024-02-21)

主引用文献

Garnett, J.A.,Martinez-Santos, V.I.,Saldana, Z.,Pape, T.,Hawthorne, W.,Chan, J.,Simpson, P.J.,Cota, E.,Puente, J.L.,Giron, J.A.,Matthews, S.
Structural insights into the biogenesis and biofilm formation by the Escherichia coli common pilus.
Proc.Natl.Acad.Sci.USA, 109:3950-3955, 2012

PubMed Abstract: Bacteria have evolved a variety of mechanisms for developing community-based biofilms. These bacterial aggregates are of clinical importance, as they are a major source of recurrent disease. Bacterial surface fibers (pili) permit adherence to biotic and abiotic substrates, often in a highly specific manner. The Escherichia coli common pilus (ECP) represents a remarkable family of extracellular fibers that are associated with both disease-causing and commensal strains. ECP plays a dual role in early-stage biofilm development and host cell recognition. Despite being the most common fimbrial structure, relatively little is known regarding its biogenesis, architecture, and function. Here we report atomic-resolution insight into the biogenesis and architecture of ECP. We also derive a structural model for entwined ECP fibers that not only illuminates interbacteria communication during biofilm formation but also provides a useful foundation for the design of novel nanofibers.

PubMed: 22355107
DOI: 10.1073/pnas.1106733109

実験手法

X-RAY DIFFRACTION (1.78 Å)