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Esben Meldgaard Høgh Quistgaard

Multispecific Substrate Recognition in a Proton-Dependent Oligopeptide Transporter

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Multispecific Substrate Recognition in a Proton-Dependent Oligopeptide Transporter. / Martinez Molledo, Maria; Quistgaard, Esben M; Flayhan, Ali; Pieprzyk, Joanna; Löw, Christian.

In: Structure, Vol. 26, No. 3, 06.03.2018, p. 467-476.e4.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Martinez Molledo, M, Quistgaard, EM, Flayhan, A, Pieprzyk, J & Löw, C 2018, 'Multispecific Substrate Recognition in a Proton-Dependent Oligopeptide Transporter', Structure, vol. 26, no. 3, pp. 467-476.e4. https://doi.org/10.1016/j.str.2018.01.005

APA

Martinez Molledo, M., Quistgaard, E. M., Flayhan, A., Pieprzyk, J., & Löw, C. (2018). Multispecific Substrate Recognition in a Proton-Dependent Oligopeptide Transporter. Structure, 26(3), 467-476.e4. https://doi.org/10.1016/j.str.2018.01.005

CBE

MLA

Vancouver

Martinez Molledo M, Quistgaard EM, Flayhan A, Pieprzyk J, Löw C. Multispecific Substrate Recognition in a Proton-Dependent Oligopeptide Transporter. Structure. 2018 Mar 6;26(3):467-476.e4. https://doi.org/10.1016/j.str.2018.01.005

Author

Martinez Molledo, Maria ; Quistgaard, Esben M ; Flayhan, Ali ; Pieprzyk, Joanna ; Löw, Christian. / Multispecific Substrate Recognition in a Proton-Dependent Oligopeptide Transporter. In: Structure. 2018 ; Vol. 26, No. 3. pp. 467-476.e4.

Bibtex

@article{35e99c3cede24374b1595f401e9844b5,
title = "Multispecific Substrate Recognition in a Proton-Dependent Oligopeptide Transporter",
abstract = "Proton-dependent oligopeptide transporters (POTs) are important for uptake of dietary di- and tripeptides in many organisms, and in humans are also involved in drug absorption. These transporters accept a wide range of substrates, but the structural basis for how different peptide side chains are accommodated has so far remained obscure. Twenty-eight peptides were screened for binding to PepTSt from Streptococcus thermophilus, and structures were determined of PepTSt in complex with four physicochemically diverse dipeptides, which bind with millimolar affinity: Ala-Leu, Phe-Ala, Ala-Gln, and Asp-Glu. The structures show that PepTSt can adapt to different peptide side chains through movement of binding site residues and water molecules, and that a good fit can be further aided by adjustment of the position of the peptide itself. Finally, structures were also determined in complex with adventitiously bound HEPES, polyethylene glycol, and phosphate molecules, which further underline the adaptability of the binding site.",
author = "{Martinez Molledo}, Maria and Quistgaard, {Esben M} and Ali Flayhan and Joanna Pieprzyk and Christian L{\"o}w",
note = "Copyright {\circledC} 2018 The Authors. Published by Elsevier Ltd.. All rights reserved.",
year = "2018",
month = "3",
day = "6",
doi = "10.1016/j.str.2018.01.005",
language = "English",
volume = "26",
pages = "467--476.e4",
journal = "Structure",
issn = "0969-2126",
publisher = "Cell Press",
number = "3",

}

RIS

TY - JOUR

T1 - Multispecific Substrate Recognition in a Proton-Dependent Oligopeptide Transporter

AU - Martinez Molledo, Maria

AU - Quistgaard, Esben M

AU - Flayhan, Ali

AU - Pieprzyk, Joanna

AU - Löw, Christian

N1 - Copyright © 2018 The Authors. Published by Elsevier Ltd.. All rights reserved.

PY - 2018/3/6

Y1 - 2018/3/6

N2 - Proton-dependent oligopeptide transporters (POTs) are important for uptake of dietary di- and tripeptides in many organisms, and in humans are also involved in drug absorption. These transporters accept a wide range of substrates, but the structural basis for how different peptide side chains are accommodated has so far remained obscure. Twenty-eight peptides were screened for binding to PepTSt from Streptococcus thermophilus, and structures were determined of PepTSt in complex with four physicochemically diverse dipeptides, which bind with millimolar affinity: Ala-Leu, Phe-Ala, Ala-Gln, and Asp-Glu. The structures show that PepTSt can adapt to different peptide side chains through movement of binding site residues and water molecules, and that a good fit can be further aided by adjustment of the position of the peptide itself. Finally, structures were also determined in complex with adventitiously bound HEPES, polyethylene glycol, and phosphate molecules, which further underline the adaptability of the binding site.

AB - Proton-dependent oligopeptide transporters (POTs) are important for uptake of dietary di- and tripeptides in many organisms, and in humans are also involved in drug absorption. These transporters accept a wide range of substrates, but the structural basis for how different peptide side chains are accommodated has so far remained obscure. Twenty-eight peptides were screened for binding to PepTSt from Streptococcus thermophilus, and structures were determined of PepTSt in complex with four physicochemically diverse dipeptides, which bind with millimolar affinity: Ala-Leu, Phe-Ala, Ala-Gln, and Asp-Glu. The structures show that PepTSt can adapt to different peptide side chains through movement of binding site residues and water molecules, and that a good fit can be further aided by adjustment of the position of the peptide itself. Finally, structures were also determined in complex with adventitiously bound HEPES, polyethylene glycol, and phosphate molecules, which further underline the adaptability of the binding site.

U2 - 10.1016/j.str.2018.01.005

DO - 10.1016/j.str.2018.01.005

M3 - Journal article

C2 - 29429879

VL - 26

SP - 467-476.e4

JO - Structure

JF - Structure

SN - 0969-2126

IS - 3

ER -