2h2p

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[[Image:2h2p.gif|left|200px]]
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{{STRUCTURE_2h2p| PDB=2h2p | SCENE= }}
{{STRUCTURE_2h2p| PDB=2h2p | SCENE= }}
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'''Crystal structure of CLC-ec1 in complex with Fab fragment in SeCN-'''
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===Crystal structure of CLC-ec1 in complex with Fab fragment in SeCN-===
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==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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(as it appears on PubMed at http://www.pubmed.gov), where 16905147 is the PubMed ID number.
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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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:47:55 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:23:29 2008''

Revision as of 12:23, 27 July 2008

Image: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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