Crystallographic characterization of the passenger domain of the Bordetella autotransporter BrkA.
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.
Zhao
Li
L
Department of Microbiology and Immunology, University of British Columbia, 2350 Health Sciences Mall, Vancouver, BC, V6T 1Z3, Canada.
Nguyen
Nham T
NT
Fernandez
Rachel C
RC
Murphy
Michael E P
ME
D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000502:physiology; D001886:Bordetella pertussis / Q000737:chemistry* / Q000235:genetics; D002942:Circular Dichroism; D003001:Cloning, Molecular; D003460:Crystallization; D003625:Data Collection; D004926:Escherichia coli / Q000235:genetics; D002479:Inclusion Bodies / Q000737:chemistry; D026901:Membrane Transport Proteins / Q000737:chemistry* / Q000235:genetics / Q000502:physiology; D008969:Molecular Sequence Data; D017510:Protein Folding; D021382:Protein Sorting Signals; D017434:Protein Structure, Tertiary / Q000235:genetics; D011506:Proteins / Q000235:genetics / Q000378:metabolism; D055571:Secretory Pathway; D017386:Sequence Homology, Amino Acid; D013223:Statistics as Topic; D013696:Temperature; D014961:X-Ray Diffraction
D001425:Bacterial Outer Membrane Proteins; C090007:BrkA protein, Bordetella pertussis; D026901:Membrane Transport Proteins; D021382:Protein Sorting Signals; D011506:Proteins