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4YB9

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

Summary for 4YB9
Entry DOI10.2210/pdb4yb9/pdb
DescriptorSolute carrier family 2, facilitated glucose transporter member 5 (1 entity in total)
Functional Keywordsglut5 transporter, fructose, bovine mfs, open inward-facing conformation, transport protein
Biological sourceBos taurus (Bovine)
Cellular locationApical cell membrane ; Multi-pass membrane protein : P58353
Total number of polymer chains1
Total formula weight52946.02
Authors
Verdon, G.,Kang, H.J.,Iwata, S.,Drew, D. (deposition date: 2015-02-18, release date: 2015-10-14, Last modification date: 2024-05-01)
Primary citationNomura, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.2 Å)
Structure validation

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数据于2024-10-30公开中

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