2exy
From Proteopedia
(New page: 200px<br /><applet load="2exy" size="450" color="white" frame="true" align="right" spinBox="true" caption="2exy, resolution 3.10Å" /> '''Crystal structure of...) |
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| - | [[Image:2exy.jpg|left|200px]]<br /><applet load="2exy" size=" | + | [[Image:2exy.jpg|left|200px]]<br /><applet load="2exy" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2exy, resolution 3.10Å" /> | caption="2exy, resolution 3.10Å" /> | ||
'''Crystal structure of the E148Q Mutant of EcClC, Fab complexed in absence of bound ions'''<br /> | '''Crystal structure of the E148Q Mutant of EcClC, Fab complexed in absence of bound ions'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The ClC channels are members of a large protein family of chloride (Cl-) | + | 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== | ||
| - | 2EXY 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:// | + | 2EXY 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=2EXY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: membrane protein/fab complex]] | [[Category: membrane protein/fab complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:15:42 2008'' |
Revision as of 15:15, 21 February 2008
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Crystal structure of the E148Q Mutant of EcClC, Fab complexed in 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
2EXY 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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