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2fee
From Proteopedia
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Structure of the Cl-/H+ exchanger CLC-ec1 from E.Coli in NaBr
Overview
CLC-ec1 is a prokaryotic CLC-type Cl(-)/H+ exchange transporter. Little is, known about the mechanism of H+ coupling to Cl-. A critical glutamate, residue, E148, was previously shown to be required for Cl(-)/H+ exchange, by mediating proton transfer between the protein and the extracellular, solution. To test whether an analogous H+ acceptor exists near the, intracellular side of the protein, we performed a mutagenesis scan of, inward-facing carboxyl-bearing residues and identified E203 as the unique, residue whose neutralization abolishes H+ coupling to Cl- transport., Glutamate at this position is strictly conserved in all known CLCs of the, transporter subclass, while valine is always found here in CLC channels., The x-ray crystal structure of the E203Q mutant is similar to that of the, wild-type protein. Cl- transport rate in E203Q is inhibited at neutral pH, and the double mutant, E148A/E203Q, shows maximal Cl- transport, independent of pH, as does the single mutant E148A. The results argue that, substrate exchange by CLC-ec1 involves two separate but partially, overlapping permeation pathways, one for Cl- and one for H+. These, pathways are congruent from the protein's extracellular surface to E148, and they diverge beyond this point toward the intracellular side. This, picture demands a transport mechanism fundamentally different from, familiar alternating-access schemes.
About this Structure
2FEE is a Single protein structure of sequence from Escherichia coli and Homo sapiens. Full crystallographic information is available from OCA.
Reference
Separate ion pathways in a Cl-/H+ exchanger., Accardi A, Walden M, Nguitragool W, Jayaram H, Williams C, Miller C, J Gen Physiol. 2005 Dec;126(6):563-70. PMID:16316975
Page seeded by OCA on Wed Nov 21 10:30:52 2007
