PDBsum entry 4yb9

Transport protein

PDB id: 4yb9

Contents

Protein chain

437 a.a.

PDB id:

4yb9

Name:

Transport protein

Title:

Crystal structure of the bovine fructose transporter glut5 in an open inward-facing conformation

Structure:

Solute carrier family 2, facilitated glucose transporter member 5. Chain: d. Synonym: fructose transporter,glucose transporter type 5,small intestine,glut-5. Engineered: yes. Mutation: yes

Source:

Bos taurus. Bovine. Organism_taxid: 9913. Gene: slc2a5, glut5. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932

Resolution:

3.20Å R-factor: 0.239 R-free: 0.258

Authors:

G.Verdon,H.J.Kang,S.Iwata,D.Drew

Key ref:

N.Nomura et al. (2015). Structure and mechanism of the mammalian fructose transporter GLUT5. Nature, 526, 397-401. PubMed id: 26416735 DOI: 10.1038/nature14909

Date:

18-Feb-15 Release date: 14-Oct-15

Protein chain

P58353  (GTR5_BOVIN) -  Solute carrier family 2, facilitated glucose transporter member 5 from Bos taurus

Seq: 501 a.a.

Struc: 437 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1038/nature14909

Nature 526:397-401 (2015)

PubMed id: 26416735

Structure and mechanism of the mammalian fructose transporter GLUT5.

N.Nomura, G.Verdon, H.J.Kang, T.Shimamura, Y.Nomura, Y.Sonoda, S.A.Hussien, A.A.Qureshi, M.Coincon, Y.Sato, H.Abe, Y.Nakada-Nakura, T.Hino, T.Arakawa, O.Kusano-Arai, H.Iwanari, T.Murata, T.Kobayashi, T.Hamakubo, M.Kasahara, S.Iwata, D.Drew.

ABSTRACT

The altered activity of the fructose transporter GLUT5, an isoform of the facilitated-diffusion glucose transporter family, has been linked to disorders such as type 2 diabetes and obesity. GLUT5 is also overexpressed in certain tumour cells, and inhibitors are potential drugs for these conditions. Here we describe the crystal structures of GLUT5 from Rattus norvegicus and Bos taurus in open outward- and open inward-facing conformations, respectively. GLUT5 has a major facilitator superfamily fold like other homologous monosaccharide transporters. On the basis of a comparison of the inward-facing structures of GLUT5 and human GLUT1, a ubiquitous glucose transporter, we show that a single point mutation is enough to switch the substrate-binding preference of GLUT5 from fructose to glucose. A comparison of the substrate-free structures of GLUT5 with occluded substrate-bound structures of Escherichia coli XylE suggests that, in addition to global rocker-switch-like re-orientation of the bundles, local asymmetric rearrangements of carboxy-terminal transmembrane bundle helices TM7 and TM10 underlie a 'gated-pore' transport mechanism in such monosaccharide transporters.