2h2p
From Proteopedia
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Crystal structure of CLC-ec1 in complex with Fab fragment in SeCN-
Overview
CLC-ec1 is a bacterial archetype of CLC transporters, a ubiquitous class, of proteins that catalyze transmembrane exchange of Cl- and H+ 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-/1 H+. In addition to Cl- and Br-, two non-halide ions, NO3- and, SCN-, are shown to be transported by CLC-ec1, but with reduced H+, counter-transport. The loss of proton coupling to these anions is, accompanied by an absence of bound anions in the central and external Cl-, binding sites in the protein's anion selectivity region, as revealed by, crystallographic comparison of Br- and SeCN- bound to this region.
About this Structure
2H2P is a Single protein structure of sequence from Escherichia coli and Mus musculus with SEK as ligand. Full crystallographic information is available from OCA.
Reference
Uncoupling of a CLC Cl-/H+ exchange transporter by polyatomic anions., Nguitragool W, Miller C, J Mol Biol. 2006 Sep 29;362(4):682-90. Epub 2006 Aug 14. PMID:16905147
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