Structures suggest a mechanism for energy coupling by a family of organic anion transporters.
Members of the solute carrier 17 (SLC17) family use divergent mechanisms to concentrate organic anions. Membrane potential drives uptake of the principal excitatory neurotransmitter glutamate into synaptic vesicles, whereas closely related proteins use proton cotransport to drive efflux from the lys...
| Main Authors: | , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2019-05-01
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| Series: | PLoS Biology |
| Online Access: | https://doi.org/10.1371/journal.pbio.3000260 |
| _version_ | 1818361435658387456 |
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| author | Jonathan B Leano Samir Batarni Jacob Eriksen Narinobu Juge John E Pak Tomomi Kimura-Someya Yaneth Robles-Colmenares Yoshinori Moriyama Robert M Stroud Robert H Edwards |
| author_facet | Jonathan B Leano Samir Batarni Jacob Eriksen Narinobu Juge John E Pak Tomomi Kimura-Someya Yaneth Robles-Colmenares Yoshinori Moriyama Robert M Stroud Robert H Edwards |
| author_sort | Jonathan B Leano |
| collection | DOAJ |
| description | Members of the solute carrier 17 (SLC17) family use divergent mechanisms to concentrate organic anions. Membrane potential drives uptake of the principal excitatory neurotransmitter glutamate into synaptic vesicles, whereas closely related proteins use proton cotransport to drive efflux from the lysosome. To delineate the divergent features of ionic coupling by the SLC17 family, we determined the structure of Escherichia coli D-galactonate/H+ symporter D-galactonate transporter (DgoT) in 2 states: one open to the cytoplasmic side and the other open to the periplasmic side with substrate bound. The structures suggest a mechanism that couples H+ flux to substrate recognition. A transition in the role of H+ from flux coupling to allostery may confer regulation by trafficking to and from the plasma membrane. |
| first_indexed | 2024-12-13T21:16:39Z |
| format | Article |
| id | doaj.art-65102fbea5e242989c390f1b3737e279 |
| institution | Directory Open Access Journal |
| issn | 1544-9173 1545-7885 |
| language | English |
| last_indexed | 2024-12-13T21:16:39Z |
| publishDate | 2019-05-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS Biology |
| spelling | doaj.art-65102fbea5e242989c390f1b3737e2792022-12-21T23:31:13ZengPublic Library of Science (PLoS)PLoS Biology1544-91731545-78852019-05-01175e300026010.1371/journal.pbio.3000260Structures suggest a mechanism for energy coupling by a family of organic anion transporters.Jonathan B LeanoSamir BatarniJacob EriksenNarinobu JugeJohn E PakTomomi Kimura-SomeyaYaneth Robles-ColmenaresYoshinori MoriyamaRobert M StroudRobert H EdwardsMembers of the solute carrier 17 (SLC17) family use divergent mechanisms to concentrate organic anions. Membrane potential drives uptake of the principal excitatory neurotransmitter glutamate into synaptic vesicles, whereas closely related proteins use proton cotransport to drive efflux from the lysosome. To delineate the divergent features of ionic coupling by the SLC17 family, we determined the structure of Escherichia coli D-galactonate/H+ symporter D-galactonate transporter (DgoT) in 2 states: one open to the cytoplasmic side and the other open to the periplasmic side with substrate bound. The structures suggest a mechanism that couples H+ flux to substrate recognition. A transition in the role of H+ from flux coupling to allostery may confer regulation by trafficking to and from the plasma membrane.https://doi.org/10.1371/journal.pbio.3000260 |
| spellingShingle | Jonathan B Leano Samir Batarni Jacob Eriksen Narinobu Juge John E Pak Tomomi Kimura-Someya Yaneth Robles-Colmenares Yoshinori Moriyama Robert M Stroud Robert H Edwards Structures suggest a mechanism for energy coupling by a family of organic anion transporters. PLoS Biology |
| title | Structures suggest a mechanism for energy coupling by a family of organic anion transporters. |
| title_full | Structures suggest a mechanism for energy coupling by a family of organic anion transporters. |
| title_fullStr | Structures suggest a mechanism for energy coupling by a family of organic anion transporters. |
| title_full_unstemmed | Structures suggest a mechanism for energy coupling by a family of organic anion transporters. |
| title_short | Structures suggest a mechanism for energy coupling by a family of organic anion transporters. |
| title_sort | structures suggest a mechanism for energy coupling by a family of organic anion transporters |
| url | https://doi.org/10.1371/journal.pbio.3000260 |
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