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3QS3

Crystal structure of the biofilm forming subunit of the E. coli common pilus: donor strand complemented (DSC) EcpA

Summary for 3QS3
Entry DOI10.2210/pdb3qs3/pdb
Related3QS2
DescriptorFimbrillin matB homolog, EcpD, CITRATE ANION (3 entities in total)
Functional Keywordspilin, ig-like fold, biofilm, adhesion, immunoglobulin-like fold, major pilin domain involved in biofilms, intermolecular and hydrophobic abiotic surface binding, extracellular membrane, fusion protein, chimera protein, cell adhesion
Biological sourceEscherichia coli
More
Total number of polymer chains12
Total formula weight243511.12
Authors
Garnett, J.A.,Matthews, S.J. (deposition date: 2011-02-19, release date: 2012-02-22, Last modification date: 2024-02-21)
Primary citationGarnett, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

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