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PDBsum entry 4kk8
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Transport protein
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PDB id
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4kk8
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Contents |
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442 a.a.
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221 a.a.
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211 a.a.
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PDB id:
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| Name: |
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Transport protein
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Title:
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Structure of the e148q mutant of clc-ec1 deltanc construct in 100mm fluoride
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Structure:
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H(+)/cl(-) exchange transporter clca. Chain: a, b. Fragment: unp residues 17-460. Synonym: clc-ec1. Engineered: yes. Mutation: yes. Fab, heavy chain. Chain: c, e. Engineered: yes.
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Source:
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Escherichia coli. Organism_taxid: 83333. Strain: k12. Gene: b0155, clca, eric, jw5012, yadq. Expressed in: escherichia coli. Expression_system_taxid: 562. Mus musculus. Organism_taxid: 10090. Expressed in: mus musculus.
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Resolution:
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2.86Å
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R-factor:
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0.212
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R-free:
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0.256
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Authors:
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H.-H.Lim,C.Miller
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Key ref:
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H.H.Lim
et al.
(2013).
Fluoride-dependent interruption of the transport cycle of a CLC Cl-/H+ antiporter.
Nat Chem Biol,
9,
721-725.
PubMed id:
DOI:
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Date:
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05-May-13
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Release date:
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21-Aug-13
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PROCHECK
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Headers
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References
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P37019
(CLCA_ECOLI) -
H(+)/Cl(-) exchange transporter ClcA from Escherichia coli (strain K12)
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Seq:
Struc:
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473 a.a.
442 a.a.*
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DOI no:
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Nat Chem Biol
9:721-725
(2013)
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PubMed id:
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Fluoride-dependent interruption of the transport cycle of a CLC Cl-/H+ antiporter.
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H.H.Lim,
R.B.Stockbridge,
C.Miller.
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ABSTRACT
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Cl(-)/H(+) antiporters of the CLC superfamily transport anions across biological
membranes in varied physiological contexts. These proteins are weakly selective
among anions commonly studied, including Cl(-), Br(-), I(-), NO3(-) and SCN(-),
but they seem to be very selective against F(-). The recent discovery of a new
CLC clade of F(-)/H(+) antiporters, which are highly selective for F(-) over
Cl(-), led us to investigate the mechanism of Cl(-)-over-F(-) selectivity by a
CLC Cl(-)/H(+) antiporter, CLC-ec1. By subjecting purified CLC-ec1 to anion
transport measurements, electrophysiological recording, equilibrium
ligand-binding studies and X-ray crystallography, we show that F(-) binds in the
Cl(-) transport pathway with affinity similar to Cl(-) but stalls the transport
cycle. Examination of various mutant antiporters implies a 'lock-down' mechanism
of F(-) inhibition, in which F(-), by virtue of its unique hydrogen-bonding
chemistry, greatly retards a proton-linked conformational change essential for
the transport cycle of CLC-ec1.
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Links
