6bqo
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='6bqo' size='340' side='right' caption='[[6bqo]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='6bqo' size='340' side='right' caption='[[6bqo]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6bqo]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BQO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BQO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6bqo]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Borpe Borpe] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BQO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BQO FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=F:FLUORIDE+ION'>F</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=F:FLUORIDE+ION'>F</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">crcB, BP1217 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=257313 BORPE])</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=6bqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bqo OCA], [http://pdbe.org/6bqo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bqo RCSB], [http://www.ebi.ac.uk/pdbsum/6bqo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bqo 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=6bqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bqo OCA], [http://pdbe.org/6bqo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bqo RCSB], [http://www.ebi.ac.uk/pdbsum/6bqo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bqo ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/CRCB_BORPE CRCB_BORPE]] Important for reducing fluoride concentration in the cell, thus reducing its toxicity. | [[http://www.uniprot.org/uniprot/CRCB_BORPE CRCB_BORPE]] Important for reducing fluoride concentration in the cell, thus reducing its toxicity. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Crystallization of dual-topology fluoride (Fluc) channels requires small, soluble crystallization chaperones known as monobodies, which act as primary crystal lattice contacts. Previous structures of Flucs have been solved in the presence of monobodies that inhibit fluoride currents in single-channel electrophysiological recordings. These structures have revealed two-fold symmetric, doubly bound arrangements, with one monobody on each side of the membrane. The combined electrophysiological and structural observations raise the possibility that chaperone binding allosterically closes the channel, altering the structure from its conducting form. To address this, we identify and solve the structure with a different monobody that only partially blocks fluoride currents. The structure of the channel-monobody complex is asymmetric, with monobody bound to one side of the channel only. The channel conformation is nearly identical on the bound and uncomplexed sides, and to all previously solved structures, providing direct structural evidence that monobody binding does not induce local structural changes. | ||
| + | |||
| + | Cork-in-Bottle Occlusion of Fluoride Ion Channels by Crystallization Chaperones.,McIlwain BC, Newstead S, Stockbridge RB Structure. 2018 Feb 22. pii: S0969-2126(18)30044-3. doi:, 10.1016/j.str.2018.02.004. PMID:29526432<ref>PMID:29526432</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6bqo" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Borpe]] | ||
| + | [[Category: Human]] | ||
[[Category: McIlwain, B C]] | [[Category: McIlwain, B C]] | ||
[[Category: Newstead, S]] | [[Category: Newstead, S]] | ||
Revision as of 07:12, 28 March 2018
Structure of a dual topology fluoride channel with monobody S8
| |||||||||||
