2ez0: Difference between revisions
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'''Crystal structure of the S107A/E148Q/Y445A mutant of EcClC, in complex with a FaB fragment''' | {{Structure | ||
|PDB= 2ez0 |SIZE=350|CAPTION= <scene name='initialview01'>2ez0</scene>, resolution 3.54Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=BR:BROMIDE ION'>BR</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Crystal structure of the S107A/E148Q/Y445A mutant of EcClC, in complex with a FaB fragment''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2EZ0 is a [ | 2EZ0 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=2EZ0 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: Lobet, S.]] | [[Category: Lobet, S.]] | ||
[[Category: BR]] | [[Category: BR]] | ||
[[Category: clc family of channels and | [[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 Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:46:10 2008'' | ||
Revision as of 17:46, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the S107A/E148Q/Y445A mutant of EcClC, in complex with a FaB fragment
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
2EZ0 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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