ArticleThe Journal of biological chemistry2011
Random mutagenesis of the prokaryotic peptide transporter YdgR identifies potential periplasmic gating residues.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 12 citations in OpenAlex.
- Functional Characterization of the Putative POT fromBiology · 2023Article
- Evidence of a Substrate-Discriminating Entrance Channel in the Lower Porter Domain of the Multidrug Resistance Efflux Pump AcrB.Antimicrobial agents and chemotherapy · 2016Article
- Salt Bridge Swapping in the EXXERFXYY Motif of Proton-coupled Oligopeptide Transporters.The Journal of biological chemistry · 2015Article
- Random mutagenesis of the multidrug transporter AcrB from Escherichia coli for identification of putative target residues of efflux pump inhibitors.Antimicrobial agents and chemotherapy · 2014Article
- Peptide transporter DtpA has two alternate conformations, one of which is promoted by inhibitor binding.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Structural insights into substrate recognition in proton-dependent oligopeptide transporters.EMBO reports · 2013Article
- Alternating access mechanism in the POT family of oligopeptide transporters.The EMBO journal · 2012Article
- Probing the putative active site of YjdL: an unusual proton-coupled oligopeptide transporter from E. coli.PloS one · 2012Article
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
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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