4YB9

Crystal structure of the Bovine Fructose transporter GLUT5 in an open inward-facing conformation

4YB9 の概要

• エントリーDOI: 10.2210/pdb4yb9/pdb
• 分子名称: Solute carrier family 2, facilitated glucose transporter member 5 (1 entity in total)
• 機能のキーワード: glut5 transporter, fructose, bovine mfs, open inward-facing conformation, transport protein
• 由来する生物種: Bos taurus (Bovine)
• 細胞内の位置: Apical cell membrane ; Multi-pass membrane protein : P58353
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 52946.02

構造登録者

Verdon, G.,Kang, H.J.,Iwata, S.,Drew, D. (登録日: 2015-02-18, 公開日: 2015-10-14, 最終更新日: 2024-05-01)

主引用文献

Nomura, N.,Verdon, G.,Kang, H.J.,Shimamura, T.,Nomura, Y.,Sonoda, Y.,Hussien, S.A.,Qureshi, A.A.,Coincon, M.,Sato, Y.,Abe, H.,Nakada-Nakura, Y.,Hino, T.,Arakawa, T.,Kusano-Arai, O.,Iwanari, H.,Murata, T.,Kobayashi, T.,Hamakubo, T.,Kasahara, M.,Iwata, S.,Drew, D.
Structure and mechanism of the mammalian fructose transporter GLUT5.
Nature, 526:397-401, 2015

PubMed 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.

PubMed: 26416735
DOI: 10.1038/nature14909

実験手法

X-RAY DIFFRACTION (3.2 Å)