2h2s: Difference between revisions

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{{STRUCTURE_2h2s|  PDB=2h2s  |  SCENE=  }}  
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'''Crystal Structure of E148A mutant of CLC-ec1 in SeCN-'''
===Crystal Structure of E148A mutant of CLC-ec1 in SeCN-===




==Overview==
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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.
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==About this Structure==
==About this Structure==
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[[Category: Clc]]
[[Category: Clc]]
[[Category: Transporter]]
[[Category: Transporter]]
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