This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

4kjp

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 06:22, 5 August 2016

Structure of the CLC-ec1 deltaNC construct in the absence of halide

Structural highlights

4kjp 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.
Related:	4kk5, 4kk6, 4kk8, 4kk9, 4kka, 4kkb, 4kjw, 4kjq
Gene:	b0155, clcA, eriC, JW5012, 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

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.

Fluoride-dependent interruption of the transport cycle of a CLC Cl/H antiporter.,Lim HH, Stockbridge RB, Miller C Nat Chem Biol. 2013 Sep 15. doi: 10.1038/nchembio.1336. PMID:24036509^[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
↑ Lim HH, Stockbridge RB, Miller C. Fluoride-dependent interruption of the transport cycle of a CLC Cl/H antiporter. Nat Chem Biol. 2013 Sep 15. doi: 10.1038/nchembio.1336. PMID:24036509 doi:http://dx.doi.org/10.1038/nchembio.1336

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/4kjp"

@@ Line 1: / Line 1: @@
 ==Structure of the CLC-ec1 deltaNC construct in the absence of halide==
 <StructureSection load='4kjp' size='340' side='right' caption='[[4kjp]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4kk5|4kk5]], [[4kk6|4kk6]], [[4kk8|4kk8]], [[4kk9|4kk9]], [[4kka|4kka]], [[4kkb|4kkb]], [[4kjw|4kjw]], [[4kjq|4kjq]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b0155, clcA, eriC, JW5012, 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=4kjp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kjp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kjp RCSB], [http://www.ebi.ac.uk/pdbsum/4kjp PDBsum]</span></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=4kjp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kjp OCA], [http://pdbe.org/4kjp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4kjp RCSB], [http://www.ebi.ac.uk/pdbsum/4kjp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4kjp ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4kjp" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4kjp

From Proteopedia

Revision as of 06:22, 5 August 2016

Structure of the CLC-ec1 deltaNC construct in the absence of halide

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox