Crystal structure of a bacterial homologue of glucose transporters GLUT1-4

Linfeng Sun, Xin Zeng, Chuangye Yan, Xiuyun Sun, Xinqi Gong, Yu Rao, Nieng Yan

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266 Scopus citations

Abstract

Glucose transporters are essential for metabolism of glucose in cells of diverse organisms from microbes to humans, exemplified by the disease-related human proteins GLUT1, 2, 3 and 4. Despite rigorous efforts, the structural information for GLUT1-4 or their homologues remains largely unknown. Here we report three related crystal structures of XylE, an Escherichia coli homologue of GLUT1-4, in complex with d-xylose, d-glucose and 6-bromo-6-deoxy-d-glucose, at resolutions of 2.8, 2.9 and 2.6Å, respectively. The structure consists of a typical major facilitator superfamily fold of 12 transmembrane segments and a unique intracellular four-helix domain. XylE was captured in an outward-facing, partly occluded conformation. Most of the important amino acids responsible for recognition of d-xylose or d-glucose are invariant in GLUT1-4, suggesting functional and mechanistic conservations. Structure-based modelling of GLUT1-4 allows mapping and interpretation of disease-related mutations. The structural and biochemical information reported here constitutes an important framework for mechanistic understanding of glucose transporters and sugar porters in general.

Original languageEnglish (US)
Pages (from-to)361-366
Number of pages6
JournalNature
Volume490
Issue number7420
DOIs
StatePublished - Oct 18 2012
Externally publishedYes

All Science Journal Classification (ASJC) codes

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    Sun, L., Zeng, X., Yan, C., Sun, X., Gong, X., Rao, Y., & Yan, N. (2012). Crystal structure of a bacterial homologue of glucose transporters GLUT1-4. Nature, 490(7420), 361-366. https://doi.org/10.1038/nature11524