Abstract
The purification and functional reconstitution of a five-component oligopeptide ATP-binding cassette transporter with a remarkably wide substrate specificity are described. High-affinity peptide uptake was dependent on liganded substrate-binding protein OppA, which interacts with the translocator OppBCDF with higher affinity than unliganded OppA. Transport screening with combinatorial peptide libraries revealed that (i) the Opp transporter is not selective with respect to amino acid side chains of the transported peptides; (ii) any peptide that can bind to OppA is transported via Opp, including very long peptides up to 35 residues long; and (iii) the binding specificity of OppA largely determines the overall transport selectivity.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Triphosphate / metabolism*
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Amino Acids / chemistry
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Bacterial Proteins
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Biological Transport
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Bradykinin / pharmacokinetics
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Carrier Proteins / chemistry*
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Carrier Proteins / metabolism
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Cell Membrane / metabolism
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Dose-Response Relationship, Drug
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Immunoblotting
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Lactococcus lactis / metabolism
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Lipoproteins / chemistry*
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Lipoproteins / metabolism
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Methionine / chemistry
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Oligopeptides / chemistry*
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Peptide Library
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Peptides / chemistry
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Plasmids / metabolism
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Protein Binding
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Protein Structure, Tertiary
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Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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Time Factors
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Valine / chemistry
Substances
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Amino Acids
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Bacterial Proteins
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Carrier Proteins
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Lipoproteins
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Oligopeptides
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Peptide Library
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Peptides
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oligopeptide-binding protein, bacteria
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Adenosine Triphosphate
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Methionine
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Valine
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Bradykinin