Unknown

Dataset Information

0

Structural evidence for induced fit and a mechanism for sugar/H+ symport in LacY.


ABSTRACT: 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.

SUBMITTER: Mirza O 

PROVIDER: S-EPMC1422171 | biostudies-literature | 2006 Mar

REPOSITORIES: biostudies-literature

altmetric image

Publications

Structural evidence for induced fit and a mechanism for sugar/H+ symport in LacY.

Mirza Osman O   Guan Lan L   Verner Gill G   Iwata So S   Kaback H Ronald HR  

The EMBO journal 20060309 6


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 indu  ...[more]

Similar Datasets

| S-EPMC1937519 | biostudies-other
| S-EPMC3918835 | biostudies-literature
| S-EPMC4882079 | biostudies-literature
| S-EPMC6969543 | biostudies-literature
| S-EPMC3021437 | biostudies-literature
| S-EPMC3249425 | biostudies-literature
| S-EPMC2654084 | biostudies-literature
| S-EPMC1370789 | biostudies-literature
| S-EPMC4000801 | biostudies-literature
| S-EPMC3710879 | biostudies-literature