3QS3
Crystal structure of the biofilm forming subunit of the E. coli common pilus: donor strand complemented (DSC) EcpA
Summary for 3QS3
| Entry DOI | 10.2210/pdb3qs3/pdb |
| Related | 3QS2 |
| Descriptor | Fimbrillin matB homolog, EcpD, CITRATE ANION (3 entities in total) |
| Functional Keywords | pilin, 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 source | Escherichia coli More |
| Total number of polymer chains | 12 |
| Total formula weight | 243511.12 |
| Authors | Garnett, J.A.,Matthews, S.J. (deposition date: 2011-02-19, release date: 2012-02-22, Last modification date: 2024-02-21) |
| Primary 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 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: 22355107DOI: 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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