Uncoupling of a CLC Cl-/H+ exchange transporter by polyatomic anions
CLC-ec1 is a bacterial archetype of CLC transporters, a ubiquitous class of proteins that catalyze transmembrane exchange of Cl{sup -} and H{sup +} necessary for pH regulation of numerous physiological processes. Despite a profusion of high-resolution structures, the molecular mechanism of exchange remains unknown. Here, we rigorously demonstrate strict exchange stoichiometry of 2 Cl{sup -}/1 H{sup +}. In addition to Cl{sup -} and Br{sup -}, two non-halide ions, NO{sub 3}{sup -} and SCN{sup -}, are shown to be transported by CLC-ec1, but with reduced H{sup +} counter-transport. The loss of proton coupling to these anions is accompanied by an absence of bound anions in the central and external Cl{sup -} binding sites in the protein's anion selectivity region, as revealed by crystallographic comparison of Br{sup -} and SeCN{sup -} bound to this region.
- Research Organization:
- Brookhaven National Lab. (BNL), Upton, NY (United States). National Synchrotron Light Source
- Sponsoring Organization:
- Doe - Office Of Science
- DOE Contract Number:
- DE-AC02-98CH10886
- OSTI ID:
- 914359
- Report Number(s):
- BNL-78927-2007-JA; JMOBAK; TRN: US0802856
- Journal Information:
- J. Mol. Biol., Vol. 362; ISSN 0022-2836
- Country of Publication:
- United States
- Language:
- English
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