Structural insights into substrate recognition in proton-dependent oligopeptide transporters
Short-chain peptides are transported across membranes through promiscuous proton-dependent oligopeptide transporters (POTs)—a subfamily of the major facilitator superfamily (MFS). The human POTs, PEPT1 and PEPT2, are also involved in the absorption of various drugs in the gut as well as transport to...
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sg-ntu-dr.10356-990882023-02-28T17:04:43Z Structural insights into substrate recognition in proton-dependent oligopeptide transporters Quistgaard, Esben M. Jong, Agnes Jin Oi Nordlund, Pär Löw, Christian Guettou, Fatma Trésaugues, Lionel Moberg, Per Jegerschöld, Caroline Zhu, Lin School of Biological Sciences Short-chain peptides are transported across membranes through promiscuous proton-dependent oligopeptide transporters (POTs)—a subfamily of the major facilitator superfamily (MFS). The human POTs, PEPT1 and PEPT2, are also involved in the absorption of various drugs in the gut as well as transport to target cells. Here, we present a structure of an oligomeric POT transporter from Shewanella oneidensis (PepTSo2), which was crystallized in the inward open conformation in complex with the peptidomimetic alafosfalin. All ligand-binding residues are highly conserved and the structural insights presented here are therefore likely to also apply to human POTs. Published version 2013-07-31T06:19:19Z 2019-12-06T20:03:09Z 2013-07-31T06:19:19Z 2019-12-06T20:03:09Z 2013 2013 Journal Article Guettou, F., Quistgaard, E. M., Trésaugues, L., Moberg, P., Jegerschöld, C., Zhu, L., Jong, A. J. O., Nordlund, P.,& Löw, C. (2013). Structural insights into substrate recognition in proton-dependent oligopeptide transporters. EMBO reports,14(9), 749-845. https://hdl.handle.net/10356/99088 http://hdl.handle.net/10220/12615 10.1038/embor.2013.107 23867627 en EMBO reports © 2013 EUROPEAN MOLECULAR BIOLOGY ORGANIZATION. This paper was published in EMBO reports and is made available as an electronic reprint (preprint) with permission of EUROPEAN MOLECULAR BIOLOGY ORGANIZATION. The paper can be found at the following official DOI: http://dx.doi.org/10.1038/embor.2013.107. One print or electronic copy may be made for personal use only. Systematic or multiple reproduction, distribution to multiple locations via electronic or other means, duplication of any material in this paper for a fee or for commercial purposes, or modification of the content of the paper is prohibited and is subject to penalties under law. application/pdf |
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Short-chain peptides are transported across membranes through promiscuous proton-dependent oligopeptide transporters (POTs)—a subfamily of the major facilitator superfamily (MFS). The human POTs, PEPT1 and PEPT2, are also involved in the absorption of various drugs in the gut as well as transport to target cells. Here, we present a structure of an oligomeric POT transporter from Shewanella oneidensis (PepTSo2), which was crystallized in the inward open conformation in complex with the peptidomimetic alafosfalin. All ligand-binding residues are highly conserved and the structural insights presented here are therefore likely to also apply to human POTs. |
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School of Biological Sciences |
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School of Biological Sciences Quistgaard, Esben M. Jong, Agnes Jin Oi Nordlund, Pär Löw, Christian Guettou, Fatma Trésaugues, Lionel Moberg, Per Jegerschöld, Caroline Zhu, Lin |
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Quistgaard, Esben M. Jong, Agnes Jin Oi Nordlund, Pär Löw, Christian Guettou, Fatma Trésaugues, Lionel Moberg, Per Jegerschöld, Caroline Zhu, Lin |
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Quistgaard, Esben M. Jong, Agnes Jin Oi Nordlund, Pär Löw, Christian Guettou, Fatma Trésaugues, Lionel Moberg, Per Jegerschöld, Caroline Zhu, Lin Structural insights into substrate recognition in proton-dependent oligopeptide transporters |
author_sort |
Quistgaard, Esben M. |
title |
Structural insights into substrate recognition in proton-dependent oligopeptide transporters |
title_short |
Structural insights into substrate recognition in proton-dependent oligopeptide transporters |
title_full |
Structural insights into substrate recognition in proton-dependent oligopeptide transporters |
title_fullStr |
Structural insights into substrate recognition in proton-dependent oligopeptide transporters |
title_full_unstemmed |
Structural insights into substrate recognition in proton-dependent oligopeptide transporters |
title_sort |
structural insights into substrate recognition in proton-dependent oligopeptide transporters |
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2013 |
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https://hdl.handle.net/10356/99088 http://hdl.handle.net/10220/12615 |
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1759856238756102144 |