1pw4
From Proteopedia
Line 1: | Line 1: | ||
[[Image:1pw4.jpg|left|200px]] | [[Image:1pw4.jpg|left|200px]] | ||
- | + | <!-- | |
- | + | The line below this paragraph, containing "STRUCTURE_1pw4", creates the "Structure Box" on the page. | |
- | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
- | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
- | + | or leave the SCENE parameter empty for the default display. | |
- | + | --> | |
- | + | {{STRUCTURE_1pw4| PDB=1pw4 | SCENE= }} | |
- | + | ||
- | | | + | |
- | }} | + | |
'''Crystal Structure of the Glycerol-3-Phosphate Transporter from E.Coli''' | '''Crystal Structure of the Glycerol-3-Phosphate Transporter from E.Coli''' | ||
Line 30: | Line 27: | ||
[[Category: Song, J.]] | [[Category: Song, J.]] | ||
[[Category: Wang, D N.]] | [[Category: Wang, D N.]] | ||
- | [[Category: | + | [[Category: Glycerol-3-phosphate]] |
- | [[Category: | + | [[Category: Inner membrane]] |
- | [[Category: | + | [[Category: Major facilitator superfamily]] |
- | [[Category: | + | [[Category: Secondary active membrane transporter]] |
- | [[Category: | + | [[Category: Transmembrane]] |
- | [[Category: | + | [[Category: Transporter]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:33:13 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 02:33, 3 May 2008
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