Crystallization of the oligopeptide-binding protein AppA from Bacillus subtilis

L  Wright; E  Blagova; V M  Levdikov; J A  Brannigan; R J  Pattenden; J  Chambers; A J  Wilkinson

doi:10.1107/S0907444903025320

Crystallization of the oligopeptide-binding protein AppA from Bacillus subtilis

L Wright, E Blagova, V M Levdikov, J A Brannigan, R J Pattenden, J Chambers, A J Wilkinson

Chemistry

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	175-177
Number of pages	3
Journal	Acta Crystallographica. Section D, Biological Crystallography
Volume	60
Issue number	1
DOIs	https://doi.org/10.1107/S0907444903025320
Publication status	Published - Jan 2004

Bibliographical note

Keywords

PEPTIDE BINDING
ESCHERICHIA-COLI
TRANSPORT-SYSTEM
OPPA PROTEIN
PHOSPHATASES
SPORULATION
PHEROMONE
BACTERIA
RECEPTOR
CIRCUIT

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10.1107/S0907444903025320

branniganja14.pdf

http://www.iucr.org/cgi-bin/paper?cy5013

Cite this

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title = "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.",

keywords = "PEPTIDE BINDING, ESCHERICHIA-COLI, TRANSPORT-SYSTEM, OPPA PROTEIN, PHOSPHATASES, SPORULATION, PHEROMONE, BACTERIA, RECEPTOR, CIRCUIT",

author = "L Wright and E Blagova and Levdikov, {V M} and Brannigan, {J A} and Pattenden, {R J} and J Chambers and Wilkinson, {A J}",

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T1 - Crystallization of the oligopeptide-binding protein AppA from Bacillus subtilis

AU - Wright, L

AU - Blagova, E

AU - Levdikov, V M

AU - Brannigan, J A

AU - Pattenden, R J

AU - Chambers, J

AU - Wilkinson, A J

PY - 2004/1

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KW - ESCHERICHIA-COLI

KW - TRANSPORT-SYSTEM

KW - OPPA PROTEIN

KW - PHOSPHATASES

KW - SPORULATION

KW - PHEROMONE

KW - BACTERIA

KW - RECEPTOR

KW - CIRCUIT

U2 - 10.1107/S0907444903025320

DO - 10.1107/S0907444903025320

M3 - Article

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SP - 175

EP - 177

JO - Acta Crystallographica. Section D, Biological Crystallography

JF - Acta Crystallographica. Section D, Biological Crystallography

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