Crystallization of the oligopeptide-binding protein AppA from Bacillus subtilis

Wright, L, Blagova, E, Levdikov, V M, Brannigan, J A, Pattenden, R J, Chambers, J and Wilkinson, A J (2004) Crystallization of the oligopeptide-binding protein AppA from Bacillus subtilis. Acta Crystallographica Section D: Biological Crystallography. pp. 175-177. ISSN 0907-4449

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Published Version: http://dx.doi.org/10.1107/S0907444903025320

Abstract

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 morpholino-ethanesulfonic acid-buffered solutions at pH 6.5 containing polyethylene glycol and zinc acetate. A complete X-ray diffraction data set extending to 2.3 Angstrom spacing has been collected.

Item Type:	Article
Copyright, Publisher and Additional Information:	Copyright © 2004 International Union of Crystallography - http://www.iucr.org/cgi-bin/paper?cy5013
Keywords:	PEPTIDE BINDING, ESCHERICHIA-COLI, TRANSPORT-SYSTEM, OPPA PROTEIN, PHOSPHATASES, SPORULATION, PHEROMONE, BACTERIA, RECEPTOR, CIRCUIT
Academic Units:	The University of York > Chemistry (York)
Depositing User:	Sherpa Assistant
Date Deposited:	11 May 2005
Last Modified:	19 Feb 2013 11:55
Published Version:	http://dx.doi.org/10.1107/S0907444903025320
Status:	Published
Refereed:	Yes
Related URLs:	http://www.iucr.org/cgi-bin/paper?cy5013
URI:	http://eprints.whiterose.ac.uk/id/eprint/457

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