2ez0
From Proteopedia
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|PDB= 2ez0 |SIZE=350|CAPTION= <scene name='initialview01'>2ez0</scene>, resolution 3.54Å | |PDB= 2ez0 |SIZE=350|CAPTION= <scene name='initialview01'>2ez0</scene>, resolution 3.54Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=BR:BROMIDE ION'>BR</scene> | + | |LIGAND= <scene name='pdbligand=BR:BROMIDE+ION'>BR</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1ots|1OTS]], [[2exw|2EXW]], [[2exy|2EXY]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ez0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ez0 OCA], [http://www.ebi.ac.uk/pdbsum/2ez0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ez0 RCSB]</span> | ||
}} | }} | ||
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[[Category: Dutzler, R.]] | [[Category: Dutzler, R.]] | ||
[[Category: Lobet, S.]] | [[Category: Lobet, S.]] | ||
| - | [[Category: BR]] | ||
[[Category: clc family of channels and transporter]] | [[Category: clc family of channels and transporter]] | ||
[[Category: h+/cl- antiporter]] | [[Category: h+/cl- antiporter]] | ||
[[Category: membrane protein/fab complex]] | [[Category: membrane protein/fab complex]] | ||
| - | ''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 02:55:40 2008'' |
Revision as of 23:55, 30 March 2008
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| , resolution 3.54Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Related: | 1OTS, 2EXW, 2EXY
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the S107A/E148Q/Y445A mutant of EcClC, in complex with a FaB fragment
Overview
The ClC channels are members of a large protein family of chloride (Cl-) channels and secondary active Cl- transporters. Despite their diverse functions, the transmembrane architecture within the family is conserved. Here we present a crystallographic study on the ion-binding properties of the ClC selectivity filter in the close homolog from Escherichia coli (EcClC). The ClC selectivity filter contains three ion-binding sites that bridge the extra- and intracellular solutions. The sites bind Cl- ions with mM affinity. Despite their close proximity within the filter, the three sites can be occupied simultaneously. The ion-binding properties are found conserved from the bacterial transporter EcClC to the human Cl- channel ClC-1, suggesting a close functional link between ion permeation in the channels and active transport in the transporters. In resemblance to K+ channels, ions permeate the ClC channel in a single file, with mutual repulsion between the ions fostering rapid conduction.
About this Structure
2EZ0 is a Single protein structure of sequence from Escherichia coli and Mus musculus. Full crystallographic information is available from OCA.
Reference
Ion-binding properties of the ClC chloride selectivity filter., Lobet S, Dutzler R, EMBO J. 2006 Jan 11;25(1):24-33. Epub 2005 Dec 8. PMID:16341087
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