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4GBY

The structure of the MFS (major facilitator superfamily) proton:xylose symporter XylE bound to D-xylose

Summary for 4GBY
Entry DOI10.2210/pdb4gby/pdb
Related4GBZ 4GC0
DescriptorD-xylose-proton symporter, beta-D-xylopyranose, nonyl beta-D-glucopyranoside, ... (4 entities in total)
Functional Keywordsmfs, d-xylose:proton symporter, transport protein
Biological sourceEscherichia coli
Total number of polymer chains1
Total formula weight55018.34
Authors
Sun, L.F.,Zeng, X.,Yan, C.Y.,Yan, N. (deposition date: 2012-07-28, release date: 2012-10-17, Last modification date: 2024-02-28)
Primary citationSun, L.,Zeng, X.,Yan, C.,Sun, X.,Gong, X.,Rao, Y.,Yan, N.
Crystal structure of a bacterial homologue of glucose transporters GLUT1-4.
Nature, 490:361-366, 2012
Cited by
PubMed 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 2.6 Å, 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.
PubMed: 23075985
DOI: 10.1038/nature11524
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.808 Å)
Structure validation

226707

数据于2024-10-30公开中

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