2h2p: Difference between revisions
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'''Crystal structure of CLC-ec1 in complex with Fab fragment in SeCN-''' | '''Crystal structure of CLC-ec1 in complex with Fab fragment in SeCN-''' | ||
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[[Category: Miller, C.]] | [[Category: Miller, C.]] | ||
[[Category: Nguitragool, W.]] | [[Category: Nguitragool, W.]] | ||
[[Category: | [[Category: Antiport]] | ||
[[Category: | [[Category: Chloride]] | ||
[[Category: | [[Category: Clc]] | ||
[[Category: | [[Category: Transporter]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:47:55 2008'' | |||
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Revision as of 02:47, 4 May 2008
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. 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 Page seeded by OCA on Sun May 4 05:47:55 2008
