1pw4

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[[Image:1pw4.jpg|left|200px]]
[[Image:1pw4.jpg|left|200px]]
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{{Structure
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|PDB= 1pw4 |SIZE=350|CAPTION= <scene name='initialview01'>1pw4</scene>, resolution 3.3&Aring;
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The line below this paragraph, containing "STRUCTURE_1pw4", creates the "Structure Box" on the page.
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|GENE= glpT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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{{STRUCTURE_1pw4| PDB=1pw4 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pw4 OCA], [http://www.ebi.ac.uk/pdbsum/1pw4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pw4 RCSB]</span>
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'''Crystal Structure of the Glycerol-3-Phosphate Transporter from E.Coli'''
'''Crystal Structure of the Glycerol-3-Phosphate Transporter from E.Coli'''
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[[Category: Song, J.]]
[[Category: Song, J.]]
[[Category: Wang, D N.]]
[[Category: Wang, D N.]]
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[[Category: glycerol-3-phosphate]]
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[[Category: Glycerol-3-phosphate]]
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[[Category: inner membrane]]
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[[Category: Inner membrane]]
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[[Category: major facilitator superfamily]]
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[[Category: Major facilitator superfamily]]
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[[Category: secondary active membrane transporter]]
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[[Category: Secondary active membrane transporter]]
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[[Category: transmembrane]]
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[[Category: Transmembrane]]
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[[Category: transporter]]
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[[Category: Transporter]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:05:19 2008''
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Revision as of 02:33, 3 May 2008

Template:STRUCTURE 1pw4

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 Page seeded by OCA on Sat May 3 05:33:13 2008

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