4QIQ

Crystal structure of D-xylose-proton symporter

Summary for 4QIQ

• Entry DOI: 10.2210/pdb4qiq/pdb
• Descriptor: D-xylose-proton symporter, ZINC ION (2 entities in total)
• Functional Keywords: membrane protein, transport protein, major facilitator superfamily (mfs), sugar transporter, membrane
• Biological source: Escherichia coli
• Cellular location: Cell inner membrane; Multi-pass membrane protein: P0AGF4
• Total number of polymer chains: 1
• Total formula weight: 52251.44

Authors

Wisedchaisri, G.,Park, M.,Iadanza, M.G.,Zheng, H.,Gonen, T. (deposition date: 2014-06-01, release date: 2014-08-06, Last modification date: 2023-09-20)

Primary citation

Wisedchaisri, G.,Park, M.S.,Iadanza, M.G.,Zheng, H.,Gonen, T.
Proton-coupled sugar transport in the prototypical major facilitator superfamily protein XylE.
Nat Commun, 5:4521-4521, 2014

PubMed 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.

PubMed: 25088546
DOI: 10.1038/ncomms5521

Experimental method

X-RAY DIFFRACTION (3.51 Å)