Structural highlights
Function
[XYLE_ECOLI] Uptake of D-xylose across the boundary membrane with the concomitant transport of protons into the cell (symport system).
Publication Abstract from PubMed
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.
Proton-coupled sugar transport in the prototypical major facilitator superfamily protein XylE.,Wisedchaisri G, Park MS, Iadanza MG, Zheng H, Gonen T Nat Commun. 2014 Aug 4;5:4521. doi: 10.1038/ncomms5521. PMID:25088546[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wisedchaisri G, Park MS, Iadanza MG, Zheng H, Gonen T. Proton-coupled sugar transport in the prototypical major facilitator superfamily protein XylE. Nat Commun. 2014 Aug 4;5:4521. doi: 10.1038/ncomms5521. PMID:25088546 doi:http://dx.doi.org/10.1038/ncomms5521
