2h2p
From Proteopedia
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| - | [[Image:2h2p.gif|left|200px]] | + | [[Image:2h2p.gif|left|200px]] |
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| - | '''Crystal structure of CLC-ec1 in complex with Fab fragment in SeCN-''' | + | {{Structure |
| + | |PDB= 2h2p |SIZE=350|CAPTION= <scene name='initialview01'>2h2p</scene>, resolution 3.100Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SEK:SELENOCYANATE ION'>SEK</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= clcA, eriC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of CLC-ec1 in complex with Fab fragment in SeCN-''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2H2P is a [ | + | 2H2P is a [[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]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H2P OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16905147 16905147] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
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[[Category: clc; transporter; chloride; antiport]] | [[Category: clc; transporter; chloride; antiport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:11:52 2008'' |
Revision as of 15:11, 20 March 2008
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| , resolution 3.100Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | clcA, eriC (Escherichia coli) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Thu Mar 20 17:11:52 2008
