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[[Image:1kpl.gif|left|200px]]


{{Structure
==Crystal Structure of the ClC Chloride Channel from S. typhimurium==
|PDB= 1kpl |SIZE=350|CAPTION= <scene name='initialview01'>1kpl</scene>, resolution 3.00&Aring;
<StructureSection load='1kpl' size='340' side='right'caption='[[1kpl]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <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>
<table><tr><td colspan='2'>[[1kpl]] is a 4 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=1KPL FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kpl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kpl OCA], [https://pdbe.org/1kpl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kpl RCSB], [https://www.ebi.ac.uk/pdbsum/1kpl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kpl ProSAT]</span></td></tr>
|RELATEDENTRY=[[1kpk|1KPK]]
</table>
|RESOURCES=<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.ebi.ac.uk/pdbsum/1kpl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kpl RCSB]</span>
== Function ==
}}
[https://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 ==
'''Crystal Structure of the ClC Chloride Channel from S. typhimurium'''
[[Image:Consurf_key_small.gif|200px|right]]
 
Check<jmol>
 
  <jmolCheckbox>
==Overview==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kp/1kpl_consurf.spt"</scriptWhenChecked>
The 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.
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==About this Structure==
  </jmolCheckbox>
1KPL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KPL OCA].  
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1kpl ConSurf].
 
<div style="clear:both"></div>
==Reference==
== References ==
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:[http://www.ncbi.nlm.nih.gov/pubmed/11796999 11796999]
<references/>
[[Category: Salmonella typhimurium]]
__TOC__
[[Category: Single protein]]
</StructureSection>
[[Category: Cadene, M.]]
[[Category: Large Structures]]
[[Category: Campbell, E B.]]
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
[[Category: Chait, B T.]]
[[Category: Cadene M]]
[[Category: Dutzler, R.]]
[[Category: Campbell EB]]
[[Category: MacKinnon, R.]]
[[Category: Chait BT]]
[[Category: helical membrane protein]]
[[Category: Dutzler R]]
[[Category: homodimer]]
[[Category: MacKinnon R]]
[[Category: ion channel]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:51:47 2008''

Latest revision as of 10:26, 14 February 2024

Crystal Structure of the ClC Chloride Channel from S. typhimuriumCrystal Structure of the ClC Chloride Channel from S. typhimurium

Structural highlights

1kpl is a 4 chain structure with sequence from Salmonella enterica subsp. enterica serovar Typhimurium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

References

  1. ↑ Dutzler R, Campbell EB, Cadene M, Chait BT, MacKinnon R. X-ray structure of a ClC chloride channel at 3.0 A reveals the molecular basis of anion selectivity. Nature. 2002 Jan 17;415(6869):287-94. PMID:11796999 doi:10.1038/415287a

1kpl, resolution 3.00Å

Drag the structure with the mouse to rotate

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