Crystal structure of a eukaryotic phosphate transporter

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Standard

Crystal structure of a eukaryotic phosphate transporter. / Pedersen, Bjørn Panyella; Kumar, Hemant; Waight, Andrew B; Risenmay, Aaron J; Roe-Zurz, Zygy; Chau, Bryant H; Schlessinger, Avner; Bonomi, Massimiliano; Harries, William; Sali, Andrej; Johri, Atul K; Stroud, Robert M.

In: Nature, Vol. 496, No. 7446, 25.04.2013, p. 533-536.

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

Harvard

Pedersen, BP, Kumar, H, Waight, AB, Risenmay, AJ, Roe-Zurz, Z, Chau, BH, Schlessinger, A, Bonomi, M, Harries, W, Sali, A, Johri, AK & Stroud, RM 2013, 'Crystal structure of a eukaryotic phosphate transporter', Nature, vol. 496, no. 7446, pp. 533-536. https://doi.org/10.1038/nature12042

APA

Pedersen, B. P., Kumar, H., Waight, A. B., Risenmay, A. J., Roe-Zurz, Z., Chau, B. H., Schlessinger, A., Bonomi, M., Harries, W., Sali, A., Johri, A. K., & Stroud, R. M. (2013). Crystal structure of a eukaryotic phosphate transporter. Nature, 496(7446), 533-536. https://doi.org/10.1038/nature12042

CBE

Pedersen BP, Kumar H, Waight AB, Risenmay AJ, Roe-Zurz Z, Chau BH, Schlessinger A, Bonomi M, Harries W, Sali A, Johri AK, Stroud RM. 2013. Crystal structure of a eukaryotic phosphate transporter. Nature. 496(7446):533-536. https://doi.org/10.1038/nature12042

MLA

Vancouver

Pedersen BP, Kumar H, Waight AB, Risenmay AJ, Roe-Zurz Z, Chau BH et al. Crystal structure of a eukaryotic phosphate transporter. Nature. 2013 Apr 25;496(7446):533-536. https://doi.org/10.1038/nature12042

Author

Pedersen, Bjørn Panyella ; Kumar, Hemant ; Waight, Andrew B ; Risenmay, Aaron J ; Roe-Zurz, Zygy ; Chau, Bryant H ; Schlessinger, Avner ; Bonomi, Massimiliano ; Harries, William ; Sali, Andrej ; Johri, Atul K ; Stroud, Robert M. / Crystal structure of a eukaryotic phosphate transporter. In: Nature. 2013 ; Vol. 496, No. 7446. pp. 533-536.

Bibtex

@article{8591b63561c44104b08fbb033a8af256,
title = "Crystal structure of a eukaryotic phosphate transporter",
abstract = "Phosphate is crucial for structural and metabolic needs, including nucleotide and lipid synthesis, signalling and chemical energy storage. Proton-coupled transporters of the major facilitator superfamily (MFS) are essential for phosphate uptake in plants and fungi, and also have a function in sensing external phosphate levels as transceptors. Here we report the 2.9 {\AA} structure of a fungal (Piriformospora indica) high-affinity phosphate transporter, PiPT, in an inward-facing occluded state, with bound phosphate visible in the membrane-buried binding site. The structure indicates both proton and phosphate exit pathways and suggests a modified asymmetrical 'rocker-switch' mechanism of phosphate transport. PiPT is related to several human transporter families, most notably the organic cation and anion transporters of the solute carrier family (SLC22), which are implicated in cancer-drug resistance. We modelled representative cation and anion SLC22 transporters based on the PiPT structure to surmise the structural basis for substrate binding and charge selectivity in this important family. The PiPT structure demonstrates and expands on principles of substrate transport by the MFS transporters and illuminates principles of phosphate uptake in particular.",
keywords = "Basidiomycota, Binding Sites, Crystallography, X-Ray, Eukaryotic Cells, Humans, Models, Biological, Models, Molecular, Phosphate Transport Proteins, Phosphates, Protein Conformation, Protons, Structure-Activity Relationship",
author = "Pedersen, {Bj{\o}rn Panyella} and Hemant Kumar and Waight, {Andrew B} and Risenmay, {Aaron J} and Zygy Roe-Zurz and Chau, {Bryant H} and Avner Schlessinger and Massimiliano Bonomi and William Harries and Andrej Sali and Johri, {Atul K} and Stroud, {Robert M}",
year = "2013",
month = apr,
day = "25",
doi = "10.1038/nature12042",
language = "English",
volume = "496",
pages = "533--536",
journal = "Nature",
issn = "0028-0836",
publisher = "Nature Publishing Group",
number = "7446",

}

RIS

TY - JOUR

T1 - Crystal structure of a eukaryotic phosphate transporter

AU - Pedersen, Bjørn Panyella

AU - Kumar, Hemant

AU - Waight, Andrew B

AU - Risenmay, Aaron J

AU - Roe-Zurz, Zygy

AU - Chau, Bryant H

AU - Schlessinger, Avner

AU - Bonomi, Massimiliano

AU - Harries, William

AU - Sali, Andrej

AU - Johri, Atul K

AU - Stroud, Robert M

PY - 2013/4/25

Y1 - 2013/4/25

N2 - Phosphate is crucial for structural and metabolic needs, including nucleotide and lipid synthesis, signalling and chemical energy storage. Proton-coupled transporters of the major facilitator superfamily (MFS) are essential for phosphate uptake in plants and fungi, and also have a function in sensing external phosphate levels as transceptors. Here we report the 2.9 Å structure of a fungal (Piriformospora indica) high-affinity phosphate transporter, PiPT, in an inward-facing occluded state, with bound phosphate visible in the membrane-buried binding site. The structure indicates both proton and phosphate exit pathways and suggests a modified asymmetrical 'rocker-switch' mechanism of phosphate transport. PiPT is related to several human transporter families, most notably the organic cation and anion transporters of the solute carrier family (SLC22), which are implicated in cancer-drug resistance. We modelled representative cation and anion SLC22 transporters based on the PiPT structure to surmise the structural basis for substrate binding and charge selectivity in this important family. The PiPT structure demonstrates and expands on principles of substrate transport by the MFS transporters and illuminates principles of phosphate uptake in particular.

AB - Phosphate is crucial for structural and metabolic needs, including nucleotide and lipid synthesis, signalling and chemical energy storage. Proton-coupled transporters of the major facilitator superfamily (MFS) are essential for phosphate uptake in plants and fungi, and also have a function in sensing external phosphate levels as transceptors. Here we report the 2.9 Å structure of a fungal (Piriformospora indica) high-affinity phosphate transporter, PiPT, in an inward-facing occluded state, with bound phosphate visible in the membrane-buried binding site. The structure indicates both proton and phosphate exit pathways and suggests a modified asymmetrical 'rocker-switch' mechanism of phosphate transport. PiPT is related to several human transporter families, most notably the organic cation and anion transporters of the solute carrier family (SLC22), which are implicated in cancer-drug resistance. We modelled representative cation and anion SLC22 transporters based on the PiPT structure to surmise the structural basis for substrate binding and charge selectivity in this important family. The PiPT structure demonstrates and expands on principles of substrate transport by the MFS transporters and illuminates principles of phosphate uptake in particular.

KW - Basidiomycota

KW - Binding Sites

KW - Crystallography, X-Ray

KW - Eukaryotic Cells

KW - Humans

KW - Models, Biological

KW - Models, Molecular

KW - Phosphate Transport Proteins

KW - Phosphates

KW - Protein Conformation

KW - Protons

KW - Structure-Activity Relationship

U2 - 10.1038/nature12042

DO - 10.1038/nature12042

M3 - Journal article

C2 - 23542591

VL - 496

SP - 533

EP - 536

JO - Nature

JF - Nature

SN - 0028-0836

IS - 7446

ER -