Crystal structure of the hexameric traffic ATPase of the Helicobacter pylori type IV secretion system.

Yeo, H J; Savvides, S N; Herr, A B; Lanka, E; Waksman, G

Yeo, H J; Savvides, S N; Herr, A B; Lanka, E; Waksman, G.

Afiliación

Yeo HJ; Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110, USA.

Mol Cell ; 6(6): 1461-72, 2000 Dec.

Article en En | MEDLINE | ID: mdl-11163218

RESUMEN

The type IV secretion system of Helicobacter pylori consists of 10--15 proteins responsible for transport of the transforming protein CagA into target epithelial cells. Secretion of CagA crucially depends on the hexameric ATPase, HP0525, a member of the VirB11-PulE family. We present the crystal structure of a binary complex of HP0525 bound to ADP. Each monomer consists of two domains formed by the N- and C-terminal halves of the sequence. ADP is bound at the interface between the two domains. In the hexamer, the N- and C-terminal domains form two rings, which together form a chamber open on one side and closed on the other. A model is proposed in which HP0525 functions as an inner membrane pore, the closure and opening of which is regulated by ATP binding and ADP release.

Asunto(s)

Adenosina Trifosfatasas/química; Antígenos Bacterianos; Proteínas Bacterianas/química; Helicobacter pylori/enzimología; Factores de Virulencia; Adenosina Difosfato/química; Adenosina Difosfato/metabolismo; Adenosina Trifosfatasas/metabolismo; Adenosina Trifosfato/metabolismo; Secuencia de Aminoácidos; Proteínas Bacterianas/metabolismo; Sitios de Unión; Cristalografía por Rayos X; Helicobacter pylori/metabolismo; Helicobacter pylori/patogenicidad; Enlace de Hidrógeno; Proteínas de la Membrana/química; Proteínas de la Membrana/metabolismo; Modelos Biológicos; Modelos Moleculares; Datos de Secuencia Molecular; Unión Proteica; Estructura Cuaternaria de Proteína; Estructura Terciaria de Proteína; Subunidades de Proteína; Proteínas Recombinantes/química; Proteínas Recombinantes/metabolismo; Alineación de Secuencia

Buscar en Google

Añadir a Mi BVS

Imprimir

XML

PubMed Links

Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Bacterianas / Helicobacter pylori / Adenosina Trifosfatasas / Factores de Virulencia / Antígenos Bacterianos Tipo de estudio: Prognostic_studies Idioma: En Revista: Mol Cell Asunto de la revista: BIOLOGIA MOLECULAR Año: 2000 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos

Buscar en Google

Añadir a Mi BVS

Imprimir

XML

PubMed Links