Your browser doesn't support javascript.
loading
A Comparative Structure/Function Analysis of Two Type IV Pilin DNA Receptors Defines a Novel Mode of DNA Binding.
Berry, Jamie-Lee; Xu, Yingqi; Ward, Philip N; Lea, Susan M; Matthews, Stephen J; Pelicic, Vladimir.
Afiliación
  • Berry JL; MRC Centre for Molecular Bacteriology and Infection, Imperial College London, London SW7 2AZ, UK.
  • Xu Y; Centre for Structural Biology, Imperial College London, London SW7 2AZ, UK.
  • Ward PN; Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.
  • Lea SM; Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.
  • Matthews SJ; Centre for Structural Biology, Imperial College London, London SW7 2AZ, UK. Electronic address: s.j.matthews@imperial.ac.uk.
  • Pelicic V; MRC Centre for Molecular Bacteriology and Infection, Imperial College London, London SW7 2AZ, UK. Electronic address: v.pelicic@imperial.ac.uk.
Structure ; 24(6): 926-34, 2016 06 07.
Article en En | MEDLINE | ID: mdl-27161979
DNA transformation is a widespread process allowing bacteria to capture free DNA by using filamentous nano-machines composed of type IV pilins. These proteins can act as DNA receptors as demonstrated by the finding that Neisseria meningitidis ComP minor pilin has intrinsic DNA-binding ability. ComP binds DNA better when it contains the DNA-uptake sequence (DUS) motif abundant in this species genome, playing a role in its trademark ability to selectively take up its own DNA. Here, we report high-resolution structures for meningococcal ComP and Neisseria subflava ComPsub, which recognize different DUS motifs. We show that they are structurally identical type IV pilins that pack readily into filament models and display a unique DD region delimited by two disulfide bonds. Functional analysis of ComPsub defines a new mode of DNA binding involving the DD region, adapted for exported DNA receptors.
Asunto(s)
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: ADN Bacteriano / Proteínas Fimbrias / Neisseria Tipo de estudio: Prognostic_studies Idioma: En Revista: Structure Asunto de la revista: BIOLOGIA MOLECULAR / BIOQUIMICA / BIOTECNOLOGIA Año: 2016 Tipo del documento: Article Pais de publicación: Estados Unidos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: ADN Bacteriano / Proteínas Fimbrias / Neisseria Tipo de estudio: Prognostic_studies Idioma: En Revista: Structure Asunto de la revista: BIOLOGIA MOLECULAR / BIOQUIMICA / BIOTECNOLOGIA Año: 2016 Tipo del documento: Article Pais de publicación: Estados Unidos