Structural basis for substrate transport in the GLUT-homology family of monosaccharide transporters
Authors:
- Esben M QuistgaardEQEsben M Quistgaard
- Christian LöwCLChristian Löw
- Per MobergPMPer Moberg
- Lionel TrésauguesLTLionel Trésaugues
- Pär NordlundPNPär Nordlund
- 28 April 2013
- journal article
- research article
- Published by Springer Nature in Nature Structural & Molecular Biology
- Vol. 20 (6) , 766-768
Abstract
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.Keywords
This publication has 17 references indexed in Scilit:
- Alternating access mechanism in the POT family of oligopeptide transportersThe EMBO Journal, 2012
- Crystal structure of a prokaryotic homologue of the mammalian oligopeptide–proton symporters, PepT1 and PepT2The EMBO Journal, 2010
- PHENIX: a comprehensive Python-based system for macromolecular structure solutionActa Crystallographica Section D Structural Biology, 2010
- XDSActa Crystallographica Section D Structural Biology, 2010
- Jalview Version 2—a multiple sequence alignment editor and analysis workbenchBioinformatics, 2009
- Ins and Outs of Major Facilitator Superfamily AntiportersAnnual Review of Microbiology, 2008
- Phasercrystallographic softwareJournal of Applied Crystallography, 2007
- Toward the structural genomics of complexes: Crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosisProceedings of the National Academy of Sciences, 2006
- Coot: model-building tools for molecular graphicsActa Crystallographica Section D Structural Biology, 2004
- Structure and Mechanism of the Lactose Permease of Escherichia coliScience, 2003