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Crystallographic characterization of the passenger domain of the Bordetella autotransporter BrkA.

ABSTRACT: Autotransporters (ATs) are proteins that deliver effectors (the passenger domain) to the surface of Gram-negative bacteria by the type V secretion pathway. The passenger domain of BrkA, a Bordetella pertussis autotransporter mediating serum resistance and adherence, was cloned in a pET expression system and overexpressed in Escherichia coli. The gene product was correctly refolded, purified to homogeneity and crystallized. The crystals diffracted to 2.8 A resolution. The space group was assumed to be P4(1)2(1)2, with unit-cell parameters a = b = 108.19, c = 115.35 A.

SUBMITTER: Zhao L 

PROVIDER: S-EPMC2688422 | biostudies-literature | 2009 Jun

REPOSITORIES: biostudies-literature

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Crystallographic characterization of the passenger domain of the Bordetella autotransporter BrkA.

Zhao Li L   Nguyen Nham T NT   Fernandez Rachel C RC   Murphy Michael E P ME  

Acta crystallographica. Section F, Structural biology and crystallization communications 20090522 Pt 6

Autotransporters (ATs) are proteins that deliver effectors (the passenger domain) to the surface of Gram-negative bacteria by the type V secretion pathway. The passenger domain of BrkA, a Bordetella pertussis autotransporter mediating serum resistance and adherence, was cloned in a pET expression system and overexpressed in Escherichia coli. The gene product was correctly refolded, purified to homogeneity and crystallized. The crystals diffracted to 2.8 A resolution. The space group was assumed  ...[more]

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