3QS2

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

Summary for 3QS2

• Entry DOI: 10.2210/pdb3qs2/pdb
• Related: 3QS3
• Descriptor: Fimbrillin matB homolog, IODIDE ION (3 entities in total)
• Functional Keywords: 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
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 42150.03

Authors

Garnett, J.A.,Matthews, S.J. (deposition date: 2011-02-19, release date: 2012-02-22, Last modification date: 2024-02-21)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.78 Å)