1pv6: Difference between revisions
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[[Image:1pv6.gif|left|200px]] | [[Image:1pv6.gif|left|200px]] | ||
'''Crystal structure of lactose permease''' | {{Structure | ||
|PDB= 1pv6 |SIZE=350|CAPTION= <scene name='initialview01'>1pv6</scene>, resolution 3.5Å | |||
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'''Crystal structure of lactose permease''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1PV6 is a [ | 1PV6 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=1PV6 OCA]. | ||
==Reference== | ==Reference== | ||
Structure and mechanism of the lactose permease of Escherichia coli., Abramson J, Smirnova I, Kasho V, Verner G, Kaback HR, Iwata S, Science. 2003 Aug 1;301(5633):610-5. PMID:[http:// | Structure and mechanism of the lactose permease of Escherichia coli., Abramson J, Smirnova I, Kasho V, Verner G, Kaback HR, Iwata S, Science. 2003 Aug 1;301(5633):610-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12893935 12893935] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transport]] | [[Category: transport]] | ||
''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 13:29:20 2008'' | ||
Revision as of 11:29, 20 March 2008
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| 1pv6, resolution 3.5Å | |||||||||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Crystal structure of lactose permease
Overview
Membrane transport proteins that transduce free energy stored in electrochemical ion gradients into a concentration gradient are a major class of membrane proteins. We report the crystal structure at 3.5 angstroms of the Escherichia coli lactose permease, an intensively studied member of the major facilitator superfamily of transporters. The molecule is composed of N- and C-terminal domains, each with six transmembrane helices, symmetrically positioned within the permease. A large internal hydrophilic cavity open to the cytoplasmic side represents the inward-facing conformation of the transporter. The structure with a bound lactose homolog, beta-D-galactopyranosyl-1-thio-beta-D-galactopyranoside, reveals the sugar-binding site in the cavity, and residues that play major roles in substrate recognition and proton translocation are identified. We propose a possible mechanism for lactose/proton symport (co-transport) consistent with both the structure and a large body of experimental data.
About this Structure
1PV6 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structure and mechanism of the lactose permease of Escherichia coli., Abramson J, Smirnova I, Kasho V, Verner G, Kaback HR, Iwata S, Science. 2003 Aug 1;301(5633):610-5. PMID:12893935
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