2h2p
From Proteopedia
(New page: 200px<br /><applet load="2h2p" size="450" color="white" frame="true" align="right" spinBox="true" caption="2h2p, resolution 3.100Å" /> '''Crystal structure o...) |
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| - | [[Image:2h2p.gif|left|200px]]<br /><applet load="2h2p" size=" | + | [[Image:2h2p.gif|left|200px]]<br /><applet load="2h2p" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2h2p, resolution 3.100Å" /> | caption="2h2p, resolution 3.100Å" /> | ||
'''Crystal structure of CLC-ec1 in complex with Fab fragment in SeCN-'''<br /> | '''Crystal structure of CLC-ec1 in complex with Fab fragment in SeCN-'''<br /> | ||
==Overview== | ==Overview== | ||
| - | CLC-ec1 is a bacterial archetype of CLC transporters, a ubiquitous class | + | 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== | ==About this Structure== | ||
| - | 2H2P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with SEK as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2H2P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=SEK:'>SEK</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H2P OCA]. |
==Reference== | ==Reference== | ||
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[[Category: clc; transporter; chloride; antiport]] | [[Category: clc; transporter; chloride; antiport]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:37:36 2008'' |
Revision as of 15:37, 21 February 2008
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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 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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