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1pw4

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{{STRUCTURE_1pw4| PDB=1pw4 | SCENE= }}
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'''Crystal Structure of the Glycerol-3-Phosphate Transporter from E.Coli'''
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===Crystal Structure of the Glycerol-3-Phosphate Transporter from E.Coli===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 12893936 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12893936}}
==About this Structure==
==About this Structure==
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[[Category: Transmembrane]]
[[Category: Transmembrane]]
[[Category: Transporter]]
[[Category: Transporter]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:33:13 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:41:43 2008''

Revision as of 20:41, 27 July 2008

Image:1pw4.png

Template:STRUCTURE 1pw4

Crystal Structure of the Glycerol-3-Phosphate Transporter from E.Coli

Template:ABSTRACT PUBMED 12893936

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 Sun Jul 27 23:41:43 2008

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