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1pw4
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(New page: 200px<br /><applet load="1pw4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pw4, resolution 3.3Å" /> '''Crystal Structure of ...)
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Revision as of 22:03, 20 November 2007
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Crystal Structure of the Glycerol-3-Phosphate Transporter from E.Coli
Overview
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.
About this Structure
1PW4 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli., Huang Y, Lemieux MJ, Song J, Auer M, Wang DN, Science. 2003 Aug 1;301(5633):616-20. PMID:12893936
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