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Crystal structure of the Thermoplasma acidophilum protein Ta1207.
Pathare, Ganesh Ramnath; Nagy, István; Hubert, Ágnes; Thomas, Dennis R; Bracher, Andreas.
Afiliación
  • Pathare GR; Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany.
  • Nagy I; Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany.
  • Hubert Á; Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany.
  • Thomas DR; Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany.
  • Bracher A; Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany.
Acta Crystallogr F Struct Biol Commun ; 73(Pt 6): 328-335, 2017 06 01.
Article en En | MEDLINE | ID: mdl-28580920
The crystal structure of the Ta1207 protein from Thermoplasma acidophilum is reported. Ta1207 was identified in a screen for high-molecular-weight protein complexes in T. acidophilum. In solution, Ta1207 forms homopentamers of 188 kDa. The crystal structure of recombinant Ta1207 solved by Se-MAD at 2.4 Šresolution revealed a complex with fivefold symmetry. In the crystal lattice, calcium ions induce the formation of a nanocage from two pentamers. The Ta1207 protomers comprise two domains with the same novel α/ß topology. A deep pocket with a binding site for a negatively charged group suggests that Ta1207 functions as an intracellular receptor for an unknown ligand. Homologues of Ta1207 occur only in Thermoplasmatales and its function might be related to the extreme lifestyle of these archaea. The thermostable Ta1207 complex might provide a useful fivefold-symmetric scaffold for future nanotechnological applications.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Thermoplasma / Calcio / Proteínas Arqueales Tipo de estudio: Prognostic_studies Idioma: En Revista: Acta Crystallogr F Struct Biol Commun Año: 2017 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Estados Unidos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Thermoplasma / Calcio / Proteínas Arqueales Tipo de estudio: Prognostic_studies Idioma: En Revista: Acta Crystallogr F Struct Biol Commun Año: 2017 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Estados Unidos