1pw4: Difference between revisions
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'''Crystal Structure of the Glycerol-3-Phosphate Transporter from E.Coli''' | {{Structure | ||
|PDB= 1pw4 |SIZE=350|CAPTION= <scene name='initialview01'>1pw4</scene>, resolution 3.3Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= glpT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |||
}} | |||
'''Crystal Structure of the Glycerol-3-Phosphate Transporter from E.Coli''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1PW4 is a [ | 1PW4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PW4 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12893936 12893936] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transporter]] | [[Category: transporter]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:29:46 2008'' | ||
Revision as of 11:29, 20 March 2008
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| 1pw4, resolution 3.3Å | |||||||||||||
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| Gene: | glpT (Escherichia coli) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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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