Structure of Rhodococcus equi virulence-associated protein B (VapB) reveals an eight-stranded antiparallel ß-barrel consisting of two Greek-key motifs.

Geerds, Christina; Wohlmann, Jens; Haas, Albert; Niemann, Hartmut H

Geerds, Christina; Wohlmann, Jens; Haas, Albert; Niemann, Hartmut H.

Afiliación

Geerds C; Department of Chemistry, Bielefeld University, Universitaetsstrasse 25, 33615 Bielefeld, Germany.
Wohlmann J; Institute for Cell Biology, University of Bonn, Ulrich-Haberland Strasse 61a, 53121 Bonn, Germany.
Haas A; Institute for Cell Biology, University of Bonn, Ulrich-Haberland Strasse 61a, 53121 Bonn, Germany.
Niemann HH; Department of Chemistry, Bielefeld University, Universitaetsstrasse 25, 33615 Bielefeld, Germany.

Acta Crystallogr F Struct Biol Commun ; 70(Pt 7): 866-71, 2014 Jul.

Article en En | MEDLINE | ID: mdl-25005079

RESUMEN

Members of the virulence-associated protein (Vap) family from the pathogen Rhodococcus equi regulate virulence in an unknown manner. They do not share recognizable sequence homology with any protein of known structure. VapB and VapA are normally associated with isolates from pigs and horses, respectively. To contribute to a molecular understanding of Vap function, the crystal structure of a protease-resistant VapB fragment was determined at 1.4âÅ resolution. The structure was solved by SAD phasing employing the anomalous signal of one endogenous S atom and two bound Co ions with low occupancy. VapB is an eight-stranded antiparallel ß-barrel with a single helix. Structural similarity to avidins suggests a potential binding function. Unlike other eight- or ten-stranded ß-barrels found in avidins, bacterial outer membrane proteins, fatty-acid-binding proteins and lysozyme inhibitors, Vaps do not have a next-neighbour arrangement but consist of two Greek-key motifs with strand order 41238567, suggesting an unusual or even unique topology.

Asunto(s)

Proteínas Bacterianas/química; Proteínas de Unión al ADN/química; Glicoproteínas de Membrana/química; Rhodococcus equi/química; Secuencias de Aminoácidos; Avidina/química; Proteínas Bacterianas/genética; Proteínas Bacterianas/metabolismo; Cristalografía por Rayos X; Proteínas de Unión al ADN/genética; Proteínas de Unión al ADN/metabolismo; Escherichia coli/genética; Escherichia coli/metabolismo; Expresión Génica; Glicoproteínas de Membrana/genética; Glicoproteínas de Membrana/metabolismo; Modelos Moleculares; Datos de Secuencia Molecular; Estructura Secundaria de Proteína; Estructura Terciaria de Proteína; Proteínas Recombinantes/química; Proteínas Recombinantes/genética; Proteínas Recombinantes/metabolismo; Rhodococcus equi/metabolismo; Homología Estructural de Proteína

Palabras clave

Greek-key motif; Rhodococcus equi; Vap protein family; antiparallel ß-barrel; single-wavelength anomalous dispersion

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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Bacterianas / Glicoproteínas de Membrana / Rhodococcus equi / Proteínas de Unión al ADN Tipo de estudio: Risk_factors_studies Idioma: En Revista: Acta Crystallogr F Struct Biol Commun Año: 2014 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Estados Unidos

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