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Proton-coupled sugar transport in the prototypical major facilitator superfamily protein XylE.

Authors
  • Wisedchaisri, Goragot
  • Park, Min-Sun
  • Iadanza, Matthew G
  • Zheng, Hongjin
  • Gonen, Tamir
Type
Published Article
Journal
Nature Communications
Publisher
Springer Nature
Publication Date
Jan 01, 2014
Volume
5
Pages
4521–4521
Identifiers
DOI: 10.1038/ncomms5521
PMID: 25088546
Source
Medline
License
Unknown

Abstract

The major facilitator superfamily (MFS) is the largest collection of structurally related membrane proteins that transport a wide array of substrates. The proton-coupled sugar transporter XylE is the first member of the MFS that has been structurally characterized in multiple transporting conformations, including both the outward and inward-facing states. Here we report the crystal structure of XylE in a new inward-facing open conformation, allowing us to visualize the rocker-switch movement of the N-domain against the C-domain during the transport cycle. Using molecular dynamics simulation, and functional transport assays, we describe the movement of XylE that facilitates sugar translocation across a lipid membrane and identify the likely candidate proton-coupling residues as the conserved Asp27 and Arg133. This study addresses the structural basis for proton-coupled substrate transport and release mechanism for the sugar porter family of proteins.

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