2cfp

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{{STRUCTURE_2cfp| PDB=2cfp | SCENE= }}
{{STRUCTURE_2cfp| PDB=2cfp | SCENE= }}
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'''SUGAR FREE LACTOSE PERMEASE AT ACIDIC PH'''
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===SUGAR FREE LACTOSE PERMEASE AT ACIDIC PH===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_16525509}}
==About this Structure==
==About this Structure==
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[[Category: Transmembrane]]
[[Category: Transmembrane]]
[[Category: Transport mechanism]]
[[Category: Transport mechanism]]
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Revision as of 09:53, 29 July 2008

Image:2cfp.png

Template:STRUCTURE 2cfp

SUGAR FREE LACTOSE PERMEASE AT ACIDIC PH

Template:ABSTRACT PUBMED 16525509

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

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