2cfp: Difference between revisions
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[[Image:2cfp.gif|left|200px]] | [[Image:2cfp.gif|left|200px]] | ||
'''SUGAR FREE LACTOSE PERMEASE AT ACIDIC PH''' | {{Structure | ||
|PDB= 2cfp |SIZE=350|CAPTION= <scene name='initialview01'>2cfp</scene>, resolution 3.30Å | |||
|SITE= <scene name='pdbsite=AC2:Hg+Binding+Site+For+Chain+A'>AC2</scene> | |||
|LIGAND= <scene name='pdbligand=HG:MERCURY (II) ION'>HG</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''SUGAR FREE LACTOSE PERMEASE AT ACIDIC PH''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2CFP is a [ | 2CFP 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=2CFP OCA]. | ||
==Reference== | ==Reference== | ||
Structural evidence for induced fit and a mechanism for sugar/H+ symport in LacY., Mirza O, Guan L, Verner G, Iwata S, Kaback HR, EMBO J. 2006 Mar 22;25(6):1177-83. Epub 2006 Mar 9. PMID:[http:// | Structural evidence for induced fit and a mechanism for sugar/H+ symport in LacY., Mirza O, Guan L, Verner G, Iwata S, Kaback HR, EMBO J. 2006 Mar 22;25(6):1177-83. Epub 2006 Mar 9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16525509 16525509] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transport mechanism]] | [[Category: transport mechanism]] | ||
''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 16:14:50 2008'' | ||
Revision as of 14:14, 20 March 2008
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| 2cfp, resolution 3.30Å | |||||||||||||
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| Sites: | AC2 | ||||||||||||
| Ligands: | HG | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
SUGAR FREE LACTOSE PERMEASE AT ACIDIC PH
Overview
Cation-coupled active transport is an essential cellular process found ubiquitously in all living organisms. Here, we present two novel ligand-free X-ray structures of the lactose permease (LacY) of Escherichia coli determined at acidic and neutral pH, and propose a model for the mechanism of coupling between lactose and H+ translocation. No sugar-binding site is observed in the absence of ligand, and deprotonation of the key residue Glu269 is associated with ligand binding. Thus, substrate induces formation of the sugar-binding site, as well as the initial step in H+ transduction.
About this Structure
2CFP is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structural evidence for induced fit and a mechanism for sugar/H+ symport in LacY., Mirza O, Guan L, Verner G, Iwata S, Kaback HR, EMBO J. 2006 Mar 22;25(6):1177-83. Epub 2006 Mar 9. PMID:16525509
Page seeded by OCA on Thu Mar 20 16:14:50 2008
