2h2s: Difference between revisions
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[[Image:2h2s.gif|left|200px]] | [[Image:2h2s.gif|left|200px]] | ||
'''Crystal Structure of E148A mutant of CLC-ec1 in SeCN-''' | {{Structure | ||
|PDB= 2h2s |SIZE=350|CAPTION= <scene name='initialview01'>2h2s</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 E148A mutant of CLC-ec1 in SeCN-''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2H2S is a [ | 2H2S 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=2H2S 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 17:11:53 2008'' | ||
Revision as of 18:11, 20 March 2008
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| , resolution 3.100Å | |||||||
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| Ligands: | |||||||
| Gene: | clcA, eriC (Escherichia coli) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of E148A mutant of CLC-ec1 in SeCN-
OverviewOverview
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 StructureAbout this Structure
2H2S is a Single protein structure of sequence from Escherichia coli and Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
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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