4JA3

Partially occluded inward open conformation of the xylose transporter XylE from E. coli

Summary for 4JA3

• Entry DOI: 10.2210/pdb4ja3/pdb
• Related: 4JA4
• Descriptor: D-xylose-proton symporter, CADMIUM ION, LUTETIUM (III) ION (3 entities in total)
• Functional Keywords: mfs general substrate transporter, xylose transporter, transport protein
• Biological source: Escherichia coli
• Cellular location: Cell inner membrane; Multi-pass membrane protein: P0AGF4
• Total number of polymer chains: 2
• Total formula weight: 106663.86

Authors

Quistgaard, E.M.,Low, C.,Moberg, P.,Tresaugues, L.,Nordlund, P. (deposition date: 2013-02-18, release date: 2013-05-01, Last modification date: 2024-02-28)

Primary citation

Quistgaard, E.M.,Low, C.,Moberg, P.,Tresaugues, L.,Nordlund, P.
Structural basis for substrate transport in the GLUT-homology family of monosaccharide transporters.
Nat.Struct.Mol.Biol., 20:766-768, 2013

PubMed 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.

PubMed: 23624861
DOI: 10.1038/nsmb.2569

Experimental method

X-RAY DIFFRACTION (3.8 Å)