Crystallization of the oligopeptide-binding protein AppA from Bacillus subtilis

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.

Metadata

Item Type:	Article
Authors/Creators:	Wright, L Blagova, E (eb500@york.ac.uk) Levdikov, V M (vl500@york.ac.uk) Brannigan, J A (jim.brannigan@york.ac.uk) Pattenden, R J Chambers, J Wilkinson, A J https://orcid.org/0000-0003-4577-9479
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
Dates:	Published: January 2004
Institution:	The University of York
Academic Units:	The University of York > Faculty of Sciences (York) > Chemistry (York)
Depositing User:	Sherpa Assistant
Date Deposited:	11 May 2005
Last Modified:	21 Jan 2025 17:13
Published Version:	https://doi.org/10.1107/S0907444903025320
Status:	Published
Refereed:	Yes
Identification Number:	10.1107/S0907444903025320
Related URLs:	http://www.iucr.org/cgi-bin/paper?cy5013
Open Archives Initiative ID (OAI ID):	oai:eprints.whiterose.ac.uk:457

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Crystallization of the oligopeptide-binding protein AppA from Bacillus subtilis

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