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Structure and Mechanism of the Glycerol-3-Phosphate Transporter from Escherichia coli
Abstract
The major facilitator superfamily represents the largest group of secondary membrane transporters in the cell. Here we report the 3.3 angstrom resolution structure of a member of this superfamily, GlpT, which transports glycerol-3-phosphate into the cytoplasm and inorganic phosphate into the periplasm. The amino- and carboxyl-terminal halves of the protein exhibit a pseudo two-fold symmetry. Closed off to the periplasm, a centrally located substrate-translocation pore contains two arginines at its closed end, which comprise the substrate-binding site. Upon substrate binding, the protein adopts a more compact conformation. We propose that GlpT operates by a single–binding site, alternating-access mechanism through a rocker-switch type of movement.
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Pao, S. S., Paulsen, I. T., & Saier, M. H. (1998) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.62.1.1-34.1998 · Cited by 2,297
Structural basis of water-specific transport through the AQP1 water channel
Sui, H., Han, B.-G., Lee, J. K., Walian, P., & Jap, B. K. (2001) · Nature · doi:10.1038/414872a · Cited by 1,166
Cited by
The SLC2 (GLUT) family of membrane transporters
Mueckler, M., & Thorens, B. (2013) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2012.07.001 · Cited by 1,328
Glucose transporters in the 21st Century
Thorens, B., & Mueckler, M. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00712.2009 · Cited by 1,013
Functional biology of plant phosphate uptake at root and mycorrhiza interfaces
Bucher, M. (2007) · New Phytologist · doi:10.1111/j.1469-8137.2006.01935.x · Cited by 718
Protein structure prediction from sequence variation
Marks, D. S., Hopf, T. A., & Sander, C. (2012) · Nature Biotechnology · doi:10.1038/nbt.2419 · Cited by 622
von Heijne, G. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2063 · Cited by 538
Metadata
- Authors
- Huang, Y., Lemieux, M. J., Song, J., Auer, M., & Wang, D.-N.
- Venue
- Science
- Published
- 2003-08
- Volume
- 301
- Issue
- 5633
- Pages
- 616-620
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2147241123
- Cited by
- 1,016
- References
- 2
- FWCI
- 30.72
- Type
- journal article
- Language
- en
- Open access
- closed
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- Huang, Y., Lemieux, M. J., Song, J., Auer, M., & Wang, D.-N. (2003). Structure and Mechanism of the Glycerol-3-Phosphate Transporter from Escherichia coli. Science. https://doi.org/10.1126/science.1087619
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
