Structural basis for substrate transport in the GLUT-homology family of monosaccharide transporters

Nat Struct Mol Biol. 2013 Jun;20(6):766-8. doi: 10.1038/nsmb.2569. Epub 2013 Apr 28.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallography, X-Ray
  • Escherichia coli / chemistry
  • Escherichia coli / enzymology*
  • Escherichia coli / metabolism
  • Escherichia coli Proteins / chemistry*
  • Escherichia coli Proteins / metabolism*
  • Models, Molecular
  • Protein Conformation
  • Symporters / chemistry*
  • Symporters / metabolism*

Substances

  • Escherichia coli Proteins
  • Symporters
  • xylE protein, E coli

Associated data

  • PDB/4JA3
  • PDB/4JA4