Ontology highlight
ABSTRACT:
SUBMITTER: Walden M
PROVIDER: S-EPMC2151619 | biostudies-literature | 2007 Apr
REPOSITORIES: biostudies-literature
The Journal of general physiology 20070401 4
The CLC-family protein CLC-ec1, a bacterial homologue of known structure, stoichiometrically exchanges two Cl(-) for one H(+) via an unknown membrane transport mechanism. This study examines mutations at a conserved tyrosine residue, Y445, that directly coordinates a Cl(-) ion located near the center of the membrane. Mutations at this position lead to "uncoupling," such that the H(+)/Cl(-) transport ratio decreases roughly with the volume of the substituted side chain. The uncoupled proteins are ...[more]