Abstract
Di- and oligopeptide- binding protein OppAs play important roles in solute and nutrient uptake, sporulation, biofilm formation, cell wall muropeptides recycling, peptide-dependent quorum-sensing responses, adherence to host cells, and a variety of other biological processes. Soluble OppA from Thermoanaerobacter tengcongensis was expressed in Escherichia coli. The protein was found to be >95% pure with SDS-PAGE after a series of purification steps and the purity was further verified by mass spectrometry. The protein was crystallized using the sitting-drop vapour-diffusion method with PEG 400 as the precipitant. Crystal diffraction extended to 2.25 Å. The crystal belonged to space group C222(1), with unit-cell parameters of a=69.395, b=199.572, c=131.673 Å, and α=β=γ=90°.
Copyright © 2012 Elsevier Inc. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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ATP-Binding Cassette Transporters / biosynthesis
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ATP-Binding Cassette Transporters / chemistry*
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ATP-Binding Cassette Transporters / isolation & purification
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Amino Acid Sequence
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Bacterial Proteins / biosynthesis
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Bacterial Proteins / chemistry*
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Bacterial Proteins / isolation & purification
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Carrier Proteins / biosynthesis
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Carrier Proteins / chemistry*
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Carrier Proteins / isolation & purification
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Crystallography, X-Ray
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Electrophoresis, Polyacrylamide Gel
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Lipoproteins / biosynthesis
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Lipoproteins / chemistry*
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Lipoproteins / isolation & purification
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Molecular Sequence Data
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Protein Binding
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Protein Conformation
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Recombinant Proteins
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Thermoanaerobacter / metabolism*
Substances
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ATP-Binding Cassette Transporters
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Bacterial Proteins
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Carrier Proteins
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Lipoproteins
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Recombinant Proteins
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oligopeptide-binding protein, bacteria