Structure of the PapD-PapGII Pilin Complex Reveals an Open and Flexible P5 Pocket

P pili are hairlike polymeric structures that mediate binding of uropathogenic Escherichia coli to the surface of the kidney via the PapG adhesin at their tips. PapG is composed of two domains: a lectin domain at the tip of the pilus followed by a pilin domain that comprises the initial polymerizing...

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Veröffentlicht in:	Journal of Bacteriology 2012-12, Vol.194 (23), p.6390-6397
Hauptverfasser:	Ford, Bradley, Verger, Denis, Dodson, Karen, Volkan, Ender, Kostakioti, Maria, Elam, Jennifer, Pinkner, Jerome, Waksman, Gabriel, Hultgren, Scott
Format:	Artikel
Sprache:	eng
Schlagworte:	adhesins Adhesins, Escherichia coli - chemistry Bacteriology Binding sites Biological and medical sciences Crystallography, X-Ray E coli Escherichia coli - chemistry Escherichia coli Proteins - chemistry fimbriae Fimbriae Proteins - chemistry Fundamental and applied biological sciences. Psychology hydrophobicity immunoglobulins Immunology kidneys lectins Microbiology Miscellaneous Models, Molecular Molecular Chaperones - chemistry molecular dynamics Molecular Dynamics Simulation Periplasmic Proteins - chemistry polymerization Protein Conformation Protein folding Simulation uropathogenic Escherichia coli
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