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Structural basis for substrate transport in the GLUT-homo...
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Esben Meldgaard Høgh Quistgaard
Structural basis for substrate transport in the GLUT-homology family of monosaccharide transporters
Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review
DOI
- https://doi.org/10.1038/nsmb.2569
Final published version
- Esben M Quistgaard
- Christian Löw ,
- Per Moberg ,
- Lionel Trésaugues ,
- Pär Nordlund
Here we present two structures of the major facilitator (MFS) xylose transporter XylE from Escherichia coli in inward open and partially occluded inward open conformations. These structures provide key information about the transport cycle of XylE and the closely related human GLUT transporters. This is, to our knowledge, the first MFS transporter structure determined in more than one conformational state, which may establish XylE as an important MFS model protein.
| Original language | English |
|---|---|
| Journal | Nature Structural and Molecular Biology |
| Volume | 20 |
| Issue | 6 |
| Pages (from-to) | 766-8 |
| Number of pages | 3 |
| ISSN | 1545-9993 |
| DOIs | |
| Publication status | Published - Jun 2013 |
| Externally published | Yes |
- Crystallography, X-Ray, Escherichia coli, Escherichia coli Proteins, Models, Molecular, Protein Conformation, Symporters, Journal Article, Research Support, Non-U.S. Gov't
Research areas
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ID: 118859123