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2exw
From Proteopedia
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| - | [[Image:2exw.gif|left|200px]] | + | [[Image:2exw.gif|left|200px]] |
| - | + | ||
| - | '''Crystal structure of a EcClC-Fab complex in the absence of bound ions''' | + | {{Structure |
| + | |PDB= 2exw |SIZE=350|CAPTION= <scene name='initialview01'>2exw</scene>, resolution 3.20Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of a EcClC-Fab complex in the absence of bound ions''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2EXW is a [ | + | 2EXW 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=2EXW OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16341087 16341087] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
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[[Category: Dutzler, R.]] | [[Category: Dutzler, R.]] | ||
[[Category: Lobet, S.]] | [[Category: Lobet, S.]] | ||
| - | [[Category: clc family of cl- channels and | + | [[Category: clc family of cl- 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 Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:45:42 2008'' |
Revision as of 14:45, 20 March 2008
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| , resolution 3.20Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of a EcClC-Fab complex in the absence of bound ions
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
2EXW 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
Page seeded by OCA on Thu Mar 20 16:45:42 2008
