2cfp

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[[Category: transport mechanism]]
[[Category: transport mechanism]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 08:36:23 2007''
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Revision as of 08:31, 30 October 2007


2cfp, resolution 3.30Å

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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] with HG as [ligand]. Structure known Active Site: AC2. 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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