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4fg6

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Revision as of 10:15, 8 November 2017

Structure of EcCLC E148A mutant in Glutamate

Structural highlights

4fg6 is a 6 chain structure with sequence from Ecoli and Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	b0155, clcA, eriC, JW5012, SSON_0167, yadQ (ECOLI)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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]

Publication Abstract from PubMed

CLC proteins underlie muscle, kidney, bone, and other organ system function by catalyzing the transport of Cl(-) ions across cell and organellar membranes. Some CLC proteins are ion channels while others are pumps that exchange Cl(-) for H(+). The pathway through which Cl(-) ions cross the membrane has been characterized, but the transport of H(+) and the principle by which their movement is coupled to Cl(-) movement is not well understood. Here we show that H(+) transport depends not only on the presence of a specific glutamate residue but also the presence of Cl(-) ions. H(+) transport, however, can be isolated and analyzed in the absence of Cl(-) by mutating the glutamate to alanine and adding carboxylate-containing molecules to solution, consistent with the notion that H(+) transfer is mediated through the entry of a carboxylate group into the anion pathway. Cl(-) ions and carboxylate interact with each other strongly. These data support a mechanism in which the glutamate carboxylate functions as a surrogate Cl(-) ion, but it can accept a H(+) and transfer it between the external solution and the central Cl(-) binding site, coupled to the movement of 2 Cl(-) ions.

Molecular mechanism of proton transport in CLC Cl-/H+ exchange transporters.,Feng L, Campbell EB, Mackinnon R Proc Natl Acad Sci U S A. 2012 Jul 17;109(29):11699-704. Epub 2012 Jul 2. PMID:22753511^[6]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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
↑ 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
↑ 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
↑ 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
↑ 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
↑ Feng L, Campbell EB, Mackinnon R. Molecular mechanism of proton transport in CLC Cl-/H+ exchange transporters. Proc Natl Acad Sci U S A. 2012 Jul 17;109(29):11699-704. Epub 2012 Jul 2. PMID:22753511 doi:10.1073/pnas.1205764109

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4fg6"

@@ Line 3: / Line 3: @@
 <StructureSection load='4fg6' size='340' side='right' caption='[[4fg6]], [[Resolution|resolution]] 3.02&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4fg6]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FG6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FG6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4fg6]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FG6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FG6 FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fg6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fg6 OCA], [http://pdbe.org/4fg6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fg6 RCSB], [http://www.ebi.ac.uk/pdbsum/4fg6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fg6 ProSAT]</span></td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b0155, clcA, eriC, JW5012, SSON_0167, yadQ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fg6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fg6 OCA], [http://pdbe.org/4fg6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fg6 RCSB], [http://www.ebi.ac.uk/pdbsum/4fg6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fg6 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 21: / Line 22: @@
 __TOC__
 </StructureSection>
+[[Category: Ecoli]]
+[[Category: Lk3 transgenic mice]]
 [[Category: Feng, L]]
 [[Category: MacKinnon, R]]

4fg6

From Proteopedia

Revision as of 10:15, 8 November 2017

Structure of EcCLC E148A mutant in Glutamate

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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