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The statistical conformation of a highly flexible protein: small-angle X-ray scattering of S. aureus protein A.
Capp, Jo A; Hagarman, Andrew; Richardson, David C; Oas, Terrence G.
Afiliación
  • Capp JA; Department of Biochemistry, Duke University School of Medicine, Durham, NC 27710, USA.
  • Hagarman A; Department of Biochemistry, Duke University School of Medicine, Durham, NC 27710, USA.
  • Richardson DC; Department of Biochemistry, Duke University School of Medicine, Durham, NC 27710, USA.
  • Oas TG; Department of Biochemistry, Duke University School of Medicine, Durham, NC 27710, USA. Electronic address: oas@duke.edu.
Structure ; 22(8): 1184-1195, 2014 Aug 05.
Article en En | MEDLINE | ID: mdl-25087509
Staphylococcal protein A (SpA) is a multidomain protein consisting of five globular IgG binding domains separated by a conserved six- to nine-residue flexible linker. We collected SAXS data on the N-terminal protein-binding half of SpA (SpA-N) and constructs consisting of one to five domain modules in order to determine statistical conformation of this important S. aureus virulence factor. We fit the SAXS data to a scattering function based on a new polymer physics model, which provides an analytical description of the SpA-N statistical conformation. We describe a protocol for systematically determining the appropriate level of modeling to fit a SAXS data set based on goodness of fit and whether the addition of parameters improves it. In the case of SpA-N, the analytical polymer physics description provides a depiction of the statistical conformation of a flexible protein that, while lacking atomistic detail, properly reflects the information content of the data.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteína Estafilocócica A / Staphylococcus aureus / Modelos Moleculares / Biología Molecular Tipo de estudio: Prognostic_studies Idioma: En Revista: Structure Asunto de la revista: BIOLOGIA MOLECULAR / BIOQUIMICA / BIOTECNOLOGIA Año: 2014 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteína Estafilocócica A / Staphylococcus aureus / Modelos Moleculares / Biología Molecular Tipo de estudio: Prognostic_studies Idioma: En Revista: Structure Asunto de la revista: BIOLOGIA MOLECULAR / BIOQUIMICA / BIOTECNOLOGIA Año: 2014 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos