4PYP

Crystal structure of the human glucose transporter GLUT1

Summary for 4PYP

• Entry DOI: 10.2210/pdb4pyp/pdb
• Descriptor: Solute carrier family 2, facilitated glucose transporter member 1, nonyl beta-D-glucopyranoside (2 entities in total)
• Functional Keywords: membrane transporter, helix, glycosylation, transport protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 56041.53

Authors

Deng, D.,Yan, C.Y.,Xu, C.,Wu, J.P.,Sun, P.C.,Hu, M.X.,Yan, N. (deposition date: 2014-03-27, release date: 2014-05-21, Last modification date: 2023-11-08)

Primary citation

Deng, D.,Xu, C.,Sun, P.C.,Wu, J.P.,Yan, C.Y.,Hu, M.X.,Yan, N.
Crystal structure of the human glucose transporter GLUT1
Nature, 510:121-125, 2014

PubMed Abstract: The glucose transporter GLUT1 catalyses facilitative diffusion of glucose into erythrocytes and is responsible for glucose supply to the brain and other organs. Dysfunctional mutations may lead to GLUT1 deficiency syndrome, whereas overexpression of GLUT1 is a prognostic indicator for cancer. Despite decades of investigation, the structure of GLUT1 remains unknown. Here we report the crystal structure of human GLUT1 at 3.2 Å resolution. The full-length protein, which has a canonical major facilitator superfamily fold, is captured in an inward-open conformation. This structure allows accurate mapping and potential mechanistic interpretation of disease-associated mutations in GLUT1. Structure-based analysis of these mutations provides an insight into the alternating access mechanism of GLUT1 and other members of the sugar porter subfamily. Structural comparison of the uniporter GLUT1 with its bacterial homologue XylE, a proton-coupled xylose symporter, allows examination of the transport mechanisms of both passive facilitators and active transporters.

PubMed: 24847886
DOI: 10.1038/nature13306

Experimental method

X-RAY DIFFRACTION (3.166 Å)