An atomic resolution model for assembly, architecture, and function of the Dr adhesins.

Anderson, Kirstine L; Billington, Jason; Pettigrew, David; Cota, Ernesto; Simpson, Peter; Roversi, Pietro; Chen, Ho An; Urvil, Petri; du Merle, Laurence; Barlow, Paul N; Medof, M Edward; Smith, Richard A G; Nowicki, Bogdan; Le Bouguénec, Chantal; Lea, Susan M; Matthews, Stephen

Anderson, Kirstine L; Billington, Jason; Pettigrew, David; Cota, Ernesto; Simpson, Peter; Roversi, Pietro; Chen, Ho An; Urvil, Petri; du Merle, Laurence; Barlow, Paul N; Medof, M Edward; Smith, Richard A G; Nowicki, Bogdan; Le Bouguénec, Chantal; Lea, Susan M; Matthews, Stephen.

Afiliación

Anderson KL; Department of Biological Sciences, Wolfson Laboratories, Imperial College London, South Kensington, London SW7 2AZ, United Kingdom.

Mol Cell ; 15(4): 647-57, 2004 Aug 27.

Article en En | MEDLINE | ID: mdl-15327779

RESUMEN

Pathogenic bacteria possess adhesion protein complexes that play essential roles in targeting host cells and in propagating infection. Although each family of adhesion proteins is generally associated with a specific human disease, the Dr family from Escherichia coli is a notable exception, as its members are associated with both diarrheal and urinary tract infections. These proteins are reported to form both fimbrial and afimbrial structures at the bacterial cell surface and target a common host cell receptor, the decay-accelerating factor (DAF or CD55). Using the newly solved three-dimensional structure of AfaE, we have constructed a robust atomic resolution model that reveals the structural basis for assembly by donor strand complementation and for the architecture of capped surface fibers.

Asunto(s)

Adhesinas de Escherichia coli/química; Escherichia coli/química; Estructura Terciaria de Proteína; Adhesinas de Escherichia coli/genética; Adhesinas de Escherichia coli/metabolismo; Secuencia de Aminoácidos; Antígenos CD55/química; Antígenos CD55/metabolismo; Cristalografía por Rayos X; Escherichia coli/metabolismo; Escherichia coli/patogenicidad; Fimbrias Bacterianas; Humanos; Modelos Moleculares; Datos de Secuencia Molecular; Resonancia Magnética Nuclear Biomolecular; Subunidades de Proteína/química; Subunidades de Proteína/genética; Subunidades de Proteína/metabolismo; Alineación de Secuencia; Resonancia por Plasmón de Superficie

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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Estructura Terciaria de Proteína / Adhesinas de Escherichia coli / Escherichia coli Tipo de estudio: Prognostic_studies Límite: Humans Idioma: En Revista: Mol Cell Asunto de la revista: BIOLOGIA MOLECULAR Año: 2004 Tipo del documento: Article País de afiliación: Reino Unido Pais de publicación: Estados Unidos

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