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Structure and Mechanism of the Glycerol-3-Phosphate Transporter from Escherichia coli.
- Source :
-
Science . 8/1/2003, Vol. 301 Issue 5633, p616-620. 5p. 5 Diagrams, 1 Chart. - Publication Year :
- 2003
-
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. [ABSTRACT FROM AUTHOR]
- Subjects :
- *ESCHERICHIA coli
*MEMBRANE proteins
*PHOSPHATES
*CYTOPLASM
Subjects
Details
- Language :
- English
- ISSN :
- 00368075
- Volume :
- 301
- Issue :
- 5633
- Database :
- Academic Search Index
- Journal :
- Science
- Publication Type :
- Academic Journal
- Accession number :
- 10581774
- Full Text :
- https://doi.org/10.1126/science.1087619