1kpl: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1kpl]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_typhimurium Salmonella enterica subsp. enterica serovar typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KPL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KPL FirstGlance]. <br> | <table><tr><td colspan='2'>[[1kpl]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_typhimurium Salmonella enterica subsp. enterica serovar typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KPL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KPL FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MYS:PENTADECANE'>MYS</scene>, <scene name='pdbligand=OCT:N-OCTANE'>OCT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MYS:PENTADECANE'>MYS</scene>, <scene name='pdbligand=OCT:N-OCTANE'>OCT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1kpk|1kpk]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1kpk|1kpk]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kpl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kpl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1kpl RCSB], [http://www.ebi.ac.uk/pdbsum/1kpl 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=1kpl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kpl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1kpl RCSB], [http://www.ebi.ac.uk/pdbsum/1kpl PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/CLCA_SALTY CLCA_SALTY]] 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.<ref>PMID:11796999</ref> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Salmonella enterica subsp. enterica serovar typhimurium]] | [[Category: Salmonella enterica subsp. enterica serovar typhimurium]] | ||
[[Category: Cadene, M | [[Category: Cadene, M]] | ||
[[Category: Campbell, E B | [[Category: Campbell, E B]] | ||
[[Category: Chait, B T | [[Category: Chait, B T]] | ||
[[Category: Dutzler, R | [[Category: Dutzler, R]] | ||
[[Category: MacKinnon, R | [[Category: MacKinnon, R]] | ||
[[Category: Helical membrane protein]] | [[Category: Helical membrane protein]] | ||
[[Category: Homodimer]] | [[Category: Homodimer]] | ||
[[Category: Ion channel]] | [[Category: Ion channel]] | ||
[[Category: Membrane protein]] | [[Category: Membrane protein]] | ||
Revision as of 19:51, 25 December 2014
Crystal Structure of the ClC Chloride Channel from S. typhimuriumCrystal Structure of the ClC Chloride Channel from S. typhimurium
Structural highlights
Function[CLCA_SALTY] 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] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe ClC chloride channels catalyse the selective flow of Cl- ions across cell membranes, thereby regulating electrical excitation in skeletal muscle and the flow of salt and water across epithelial barriers. Genetic defects in ClC Cl- channels underlie several familial muscle and kidney diseases. Here we present the X-ray structures of two prokaryotic ClC Cl- channels from Salmonella enterica serovar typhimurium and Escherichia coli at 3.0 and 3.5 A, respectively. Both structures reveal two identical pores, each pore being formed by a separate subunit contained within a homodimeric membrane protein. Individual subunits are composed of two roughly repeated halves that span the membrane with opposite orientations. This antiparallel architecture defines a selectivity filter in which a Cl- ion is stabilized by electrostatic interactions with alpha-helix dipoles and by chemical coordination with nitrogen atoms and hydroxyl groups. These findings provide a structural basis for further understanding the function of ClC Cl- channels, and establish the physical and chemical basis of their anion selectivity. X-ray structure of a ClC chloride channel at 3.0 A reveals the molecular basis of anion selectivity.,Dutzler R, Campbell EB, Cadene M, Chait BT, MacKinnon R Nature. 2002 Jan 17;415(6869):287-94. PMID:11796999[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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