Crystallization of the oligopeptide-binding protein AppA from Bacillus subtilis

AppA is the membrane‐anchored extracellular receptor component of an ABC transporter responsible for the uptake of oligopeptides into Bacillus subtilis. AppA has been overexpressed as a cleavable maltose‐binding protein fusion in Escherichia coli. Following removal of the fusion portion, AppA has be...

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Bibliographic Details
Published in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2004-01, Vol.60 (1), p.175-177
Main Authors: Wright, Lisa, Blagova, Elena, Levdikov, Vladimir M., Brannigan, James A., Pattenden, Rebecca J., Chambers, Janet, Wilkinson, Anthony J.
Format: Article
Language:English
Subjects:
AppA
Bacillus subtilis - genetics
Bacillus subtilis - metabolism
Bacterial Proteins - chemistry
Bacterial Proteins - genetics
Carrier Proteins - chemistry
Carrier Proteins - genetics
Chromatography, Ion Exchange
Crystallization
Crystallography, X-Ray
DNA, Bacterial - chemistry
DNA, Bacterial - genetics
Escherichia coli - genetics
oligopeptide-binding proteins
Polymerase Chain Reaction
Recombinant Proteins - chemistry
Recombinant Proteins - genetics
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Summary:AppA is the membrane‐anchored extracellular receptor component of an ABC transporter responsible for the uptake of oligopeptides into Bacillus subtilis. AppA has been overexpressed as a cleavable maltose‐binding protein fusion in Escherichia coli. Following removal of the fusion portion, AppA has been crystallized from morpholinoethanesulfonic acid‐buffered solutions at pH 6.5 containing polyethylene glycol and zinc acetate. A complete X‐ray diffraction data set extending to 2.3 Å spacing has been collected.
ISSN:1399-0047
0907-4449
1399-0047
DOI:10.1107/S0907444903025320