2exy
From Proteopedia
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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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