2exw: Difference between revisions

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New page: left|200px<br /><applet load="2exw" size="450" color="white" frame="true" align="right" spinBox="true" caption="2exw, resolution 3.20Å" /> '''Crystal structure of...
 
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[[Image:2exw.gif|left|200px]]<br /><applet load="2exw" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2exw.gif|left|200px]]<br /><applet load="2exw" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2exw, resolution 3.20&Aring;" />
caption="2exw, resolution 3.20&Aring;" />
'''Crystal structure of a EcClC-Fab complex in the absence of bound ions'''<br />
'''Crystal structure of a EcClC-Fab complex in the absence of bound ions'''<br />


==Overview==
==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.
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==
==About this Structure==
2EXW is a [http://en.wikipedia.org/wiki/Single_protein 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2EXW OCA].  
2EXW is a [http://en.wikipedia.org/wiki/Single_protein 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==
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[[Category: membrane protein/fab complex]]
[[Category: membrane protein/fab complex]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:12:48 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:15:42 2008''

Revision as of 18:15, 21 February 2008

File:2exw.gif


2exw, resolution 3.20Å

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Crystal structure of a EcClC-Fab complex in the absence of bound ions

OverviewOverview

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 StructureAbout this Structure

2EXW is a Single protein structure of sequence from Escherichia coli and Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

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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