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The FapF Amyloid Secretion Transporter Possesses an Atypical Asymmetric Coiled Coil.
Rouse, Sarah L; Stylianou, Fisentzos; Wu, H Y Grace; Berry, Jamie-Lee; Sewell, Lee; Morgan, R Marc L; Sauerwein, Andrea C; Matthews, Steve.
Afiliación
  • Rouse SL; Department of Life Sciences, Imperial College London, South Kensington Campus, London SW7 2AZ, UK.
  • Stylianou F; Department of Life Sciences, Imperial College London, South Kensington Campus, London SW7 2AZ, UK.
  • Wu HYG; Department of Life Sciences, Imperial College London, South Kensington Campus, London SW7 2AZ, UK.
  • Berry JL; Department of Life Sciences, Imperial College London, South Kensington Campus, London SW7 2AZ, UK.
  • Sewell L; Department of Life Sciences, Imperial College London, South Kensington Campus, London SW7 2AZ, UK.
  • Morgan RML; Department of Life Sciences, Imperial College London, South Kensington Campus, London SW7 2AZ, UK.
  • Sauerwein AC; Department of Life Sciences, Imperial College London, South Kensington Campus, London SW7 2AZ, UK.
  • Matthews S; Department of Life Sciences, Imperial College London, South Kensington Campus, London SW7 2AZ, UK. Electronic address: s.j.matthews@imperial.ac.uk.
J Mol Biol ; 430(20): 3863-3871, 2018 10 12.
Article en En | MEDLINE | ID: mdl-29886016
Gram-negative bacteria possess specialized biogenesis machineries that facilitate the export of amyloid subunits, the fibers of which are key components of their biofilm matrix. The secretion of bacterial functional amyloid requires a specialized outer-membrane protein channel through which unfolded amyloid substrates are translocated. We previously reported the crystal structure of the membrane-spanning domain of the amyloid subunit transporter FapF from Pseudomonas. However, the structure of the periplasmic domain, which is essential for amyloid transport, is yet to be determined. Here, we present the crystal structure of the N-terminal periplasmic domain at 1.8-Å resolution. This domain forms a novel asymmetric trimeric coiled coil that possesses a single buried tyrosine residue as well as an extensive hydrogen-bonding network within a glutamine layer. This new structural insight allows us to understand this newly described functional amyloid secretion system in greater detail.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Conformación Proteica / Proteínas Bacterianas / Modelos Moleculares / Proteínas Amiloidogénicas / Amiloide Tipo de estudio: Prognostic_studies Idioma: En Revista: J Mol Biol Año: 2018 Tipo del documento: Article Pais de publicación: Países Bajos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Conformación Proteica / Proteínas Bacterianas / Modelos Moleculares / Proteínas Amiloidogénicas / Amiloide Tipo de estudio: Prognostic_studies Idioma: En Revista: J Mol Biol Año: 2018 Tipo del documento: Article Pais de publicación: Países Bajos