Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 286, Issue 26, Pages 23121-23131Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M111.239657
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Funding
- Austrian Science Fund [SFB35, F3507, F3502]
- Federal Ministry of Economy, Family and Youth through Laura Bassi Centre of Expertise initiative [253275]
- Boehringer Ingelheim
- Austrian Science Fund (FWF) [F 3507] Funding Source: researchfish
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The peptide transporter (PTR) family represents a group of proton-coupled secondary transporters responsible for bulk uptake of amino acids in the form of di- and tripeptides, an essential process employed across species ranging from bacteria to humans. To identify amino acids critical for peptide transport in a prokaryotic PTR member, we have screened a library of mutants of the Escherichia coli peptide transporter YdgR using a high-throughput substrate uptake assay. We have identified 35 single point mutations that result in a full or partial loss of transport activity. Additional analysis, including homology modeling based on the crystal structure of the Shewanella oneidensis peptide transporter PepT(so), identifies Glu(56) and Arg(305) as potential periplasmic gating residues. In addition to providing new insights into transport by members of the PTR family, these mutants provide valuable tools for further study of the mechanism of peptide transport.
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