2h2p: Difference between revisions

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[[Image:2h2p.gif|left|200px]]
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[[Image:2h2p.png|left|200px]]


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{{STRUCTURE_2h2p|  PDB=2h2p  |  SCENE=  }}  
{{STRUCTURE_2h2p|  PDB=2h2p  |  SCENE=  }}  


'''Crystal structure of CLC-ec1 in complex with Fab fragment in SeCN-'''
===Crystal structure of CLC-ec1 in complex with Fab fragment 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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{{ABSTRACT_PUBMED_16905147}}


==About this Structure==
==About this Structure==
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[[Category: Clc]]
[[Category: Clc]]
[[Category: Transporter]]
[[Category: Transporter]]
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Revision as of 12:23, 27 July 2008

File:2h2p.png

Template:STRUCTURE 2h2p

Crystal structure of CLC-ec1 in complex with Fab fragment in SeCN-

Template:ABSTRACT PUBMED 16905147

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

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