3ejz

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[[Image:3ejz.png|left|200px]]
 
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{{STRUCTURE_3ejz| PDB=3ejz | SCENE= }}
{{STRUCTURE_3ejz| PDB=3ejz | SCENE= }}
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===Structure of E203V mutant E.coli Cl-/H+ exchanger, CLC-ec1===
===Structure of E203V mutant E.coli Cl-/H+ exchanger, CLC-ec1===
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{{ABSTRACT_PUBMED_19139174}}
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{{ABSTRACT_PUBMED_19139174}}
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==Function==
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[[http://www.uniprot.org/uniprot/CLCA_ECOLI CLCA_ECOLI]] Proton-coupled chloride transporter. Functions as antiport system and exchanges two chloride ions for 1 proton. Probably acts as an electrical shunt for an outwardly-directed proton pump that is linked to amino acid decarboxylation, as part of the extreme acid resistance (XAR) response.<ref>PMID:12384697</ref> <ref>PMID:14985752</ref> <ref>PMID:16341087</ref> <ref>PMID:16905147</ref> <ref>PMID:18678918</ref>
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:019139174</ref><references group="xtra"/>
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<ref group="xtra">PMID:019139174</ref><references group="xtra"/><references/>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]

Revision as of 02:53, 20 September 2013

Template:STRUCTURE 3ejz

Contents

Structure of E203V mutant E.coli Cl-/H+ exchanger, CLC-ec1

Template:ABSTRACT PUBMED 19139174

Function

[CLCA_ECOLI] Proton-coupled chloride transporter. Functions as antiport system and exchanges two chloride ions for 1 proton. Probably acts as an electrical shunt for an outwardly-directed proton pump that is linked to amino acid decarboxylation, as part of the extreme acid resistance (XAR) response.[1] [2] [3] [4] [5]

About this Structure

3ejz is a 6 chain structure with sequence from Escherichia coli and Mus musculus. Full crystallographic information is available from OCA.

Reference

  • Lim HH, Miller C. Intracellular proton-transfer mutants in a CLC Cl-/H+ exchanger. J Gen Physiol. 2009 Feb;133(2):131-8. Epub 2009 Jan 12. PMID:19139174 doi:10.1085/jgp.200810112
  1. Iyer R, Iverson TM, Accardi A, Miller C. A biological role for prokaryotic ClC chloride channels. Nature. 2002 Oct 17;419(6908):715-8. PMID:12384697 doi:10.1038/nature01000
  2. Accardi A, Miller C. Secondary active transport mediated by a prokaryotic homologue of ClC Cl- channels. Nature. 2004 Feb 26;427(6977):803-7. PMID:14985752 doi:10.1038/nature02314
  3. Lobet S, Dutzler R. Ion-binding properties of the ClC chloride selectivity filter. EMBO J. 2006 Jan 11;25(1):24-33. Epub 2005 Dec 8. PMID:16341087
  4. Nguitragool W, Miller C. Uncoupling of a CLC Cl-/H+ exchange transporter by polyatomic anions. J Mol Biol. 2006 Sep 29;362(4):682-90. Epub 2006 Aug 14. PMID:16905147 doi:10.1016/j.jmb.2006.07.006
  5. Jayaram H, Accardi A, Wu F, Williams C, Miller C. Ion permeation through a Cl--selective channel designed from a CLC Cl-/H+ exchanger. Proc Natl Acad Sci U S A. 2008 Aug 12;105(32):11194-9. Epub 2008 Aug 4. PMID:18678918

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