View source for 4kk9


==Structure of the E148A mutant of CLC-ec1 deltaNC construct in 100mM fluoride and 2mM Bromide==
<StructureSection load='4kk9' size='340' side='right'caption='[[4kk9]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4kk9]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KK9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KK9 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.997&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4kk9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kk9 OCA], [https://pdbe.org/4kk9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kk9 RCSB], [https://www.ebi.ac.uk/pdbsum/4kk9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kk9 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== 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<ref>PMID:24036509</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4kk9" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Lim H-H]]
[[Category: Miller C]]