1kpl: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
 
(13 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1kpl.gif|left|200px]]


<!--
==Crystal Structure of the ClC Chloride Channel from S. typhimurium==
The line below this paragraph, containing "STRUCTURE_1kpl", creates the "Structure Box" on the page.
<StructureSection load='1kpl' size='340' side='right'caption='[[1kpl]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</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>
-->
<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>
{{STRUCTURE_1kpl|  PDB=1kpl  |  SCENE= }}
<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>
 
</table>
'''Crystal Structure of the ClC Chloride Channel from S. typhimurium'''
== 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 ==
==Overview==
[[Image:Consurf_key_small.gif|200px|right]]
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.
Check<jmol>
 
  <jmolCheckbox>
==About this Structure==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kp/1kpl_consurf.spt"</scriptWhenChecked>
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].  
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==Reference==
  </jmolCheckbox>
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]
</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].
[[Category: Salmonella typhimurium]]
<div style="clear:both"></div>
[[Category: Single protein]]
== References ==
[[Category: Cadene, M.]]
<references/>
[[Category: Campbell, E B.]]
__TOC__
[[Category: Chait, B T.]]
</StructureSection>
[[Category: Dutzler, R.]]
[[Category: Large Structures]]
[[Category: MacKinnon, R.]]
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
[[Category: Helical membrane protein]]
[[Category: Cadene M]]
[[Category: Homodimer]]
[[Category: Campbell EB]]
[[Category: Ion channel]]
[[Category: Chait BT]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 23:01:06 2008''
[[Category: Dutzler R]]
[[Category: MacKinnon R]]
Retrieved from "https://proteopedia.org/1kpl"