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6d0n
From Proteopedia
(Difference between revisions)
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<StructureSection load='6d0n' size='340' side='right' caption='[[6d0n]], [[Resolution|resolution]] 3.12Å' scene=''> | <StructureSection load='6d0n' size='340' side='right' caption='[[6d0n]], [[Resolution|resolution]] 3.12Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6d0n]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6D0N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6D0N FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6d0n]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Entcs Entcs] and [http://en.wikipedia.org/wiki/Synthetic_construct_sequences Synthetic construct sequences]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6D0N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6D0N FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DMU:DECYL-BETA-D-MALTOPYRANOSIDE'>DMU</scene>, <scene name='pdbligand=F:FLUORIDE+ION'>F</scene>, <scene name='pdbligand=MHA:(CARBAMOYLMETHYL-CARBOXYMETHYL-AMINO)-ACETIC+ACID'>MHA</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DMU:DECYL-BETA-D-MALTOPYRANOSIDE'>DMU</scene>, <scene name='pdbligand=F:FLUORIDE+ION'>F</scene>, <scene name='pdbligand=MHA:(CARBAMOYLMETHYL-CARBOXYMETHYL-AMINO)-ACETIC+ACID'>MHA</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ECAG_02710 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=565654 ENTCS])</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=6d0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6d0n OCA], [http://pdbe.org/6d0n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6d0n RCSB], [http://www.ebi.ac.uk/pdbsum/6d0n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6d0n ProSAT]</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=6d0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6d0n OCA], [http://pdbe.org/6d0n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6d0n RCSB], [http://www.ebi.ac.uk/pdbsum/6d0n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6d0n ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Fluoride/proton antiporters of the CLC(F) family combat F(-) toxicity in bacteria by exporting this halide from the cytoplasm. These transporters belong to the widespread CLC superfamily but display transport properties different from those of the well-studied Cl(-)/H(+) antiporters. Here, we report a structural and functional investigation of these F(-)-transport proteins. Crystal structures of a CLC(F) homolog from Enterococcus casseliflavus are captured in two conformations with simultaneous accessibility of F(-) and H(+) ions via separate pathways on opposite sides of the membrane. Manipulation of a key glutamate residue critical for H(+) and F(-) transport reverses the anion selectivity of transport; replacement of the glutamate with glutamine or alanine completely inhibits F(-) and H(+) transport while allowing for rapid uncoupled flux of Cl(-). The structural and functional results lead to a 'windmill' model of CLC antiport wherein F (-) and H(+) simultaneously move through separate ion-specific pathways that switch sidedness during the transport cycle. | ||
| + | |||
| + | A CLC-type F(-)/H(+) antiporter in ion-swapped conformations.,Last NB, Stockbridge RB, Wilson AE, Shane T, Kolmakova-Partensky L, Koide A, Koide S, Miller C Nat Struct Mol Biol. 2018 Jun 25. pii: 10.1038/s41594-018-0082-0. doi:, 10.1038/s41594-018-0082-0. PMID:29941917<ref>PMID:29941917</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6d0n" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Entcs]] | ||
| + | [[Category: Synthetic construct sequences]] | ||
[[Category: Koide, A]] | [[Category: Koide, A]] | ||
[[Category: Koide, S]] | [[Category: Koide, S]] | ||
Revision as of 06:16, 11 July 2018
Crystal structure of a CLC-type fluoride/proton antiporter, V319G mutant
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