2h2p
From Proteopedia
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|PDB= 2h2p |SIZE=350|CAPTION= <scene name='initialview01'>2h2p</scene>, resolution 3.100Å | |PDB= 2h2p |SIZE=350|CAPTION= <scene name='initialview01'>2h2p</scene>, resolution 3.100Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SEK:SELENOCYANATE ION'>SEK</scene> | + | |LIGAND= <scene name='pdbligand=SEK:SELENOCYANATE+ION'>SEK</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= clcA, eriC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= clcA, eriC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1ots|1OTS]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2h2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h2p OCA], [http://www.ebi.ac.uk/pdbsum/2h2p PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2h2p RCSB]</span> | ||
}} | }} | ||
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[[Category: Miller, C.]] | [[Category: Miller, C.]] | ||
[[Category: Nguitragool, W.]] | [[Category: Nguitragool, W.]] | ||
| - | [[Category: | + | [[Category: antiport]] |
| - | [[Category: clc | + | [[Category: chloride]] |
| + | [[Category: clc]] | ||
| + | [[Category: transporter]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:24:36 2008'' |
Revision as of 00:24, 31 March 2008
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| , resolution 3.100Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | clcA, eriC (Escherichia coli) | ||||||
| Related: | 1OTS
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
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