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| | ==Crystal structure of the CLIC homologue EXC-4 from c. elegans== | | ==Crystal structure of the CLIC homologue EXC-4 from c. elegans== |
| - | <StructureSection load='2yv9' size='340' side='right' caption='[[2yv9]], [[Resolution|resolution]] 1.60Å' scene=''> | + | <StructureSection load='2yv9' size='340' side='right'caption='[[2yv9]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2yv9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Caeel Caeel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YV9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YV9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2yv9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YV9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YV9 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1k0m|1k0m]], [[2ahe|2ahe]], [[2yu7|2yu7]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">exc-4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL])</td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2yv9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yv9 OCA], [https://pdbe.org/2yv9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yv9 RCSB], [https://www.ebi.ac.uk/pdbsum/2yv9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yv9 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=2yv9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yv9 OCA], [http://pdbe.org/2yv9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2yv9 RCSB], [http://www.ebi.ac.uk/pdbsum/2yv9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2yv9 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/EXC4_CAEEL EXC4_CAEEL]] May insert into membranes and form chloride ion channels. Involved in the formation of the excretory canal. Required to prevent cystic lumenal expansions in the excretory cell. Not required for formation of the initial tube, but is required for regulating the size of the tube lumen as it grows.<ref>PMID:17985355</ref> | + | [https://www.uniprot.org/uniprot/EXC4_CAEEL EXC4_CAEEL] May insert into membranes and form chloride ion channels. Involved in the formation of the excretory canal. Required to prevent cystic lumenal expansions in the excretory cell. Not required for formation of the initial tube, but is required for regulating the size of the tube lumen as it grows.<ref>PMID:17985355</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Ion channels|Ion channels]] | + | *[[Ion channels 3D structures|Ion channels 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Caeel]] | + | [[Category: Caenorhabditis elegans]] |
| - | [[Category: Curmi, P M.G]] | + | [[Category: Large Structures]] |
| - | [[Category: Harrop, S J]] | + | [[Category: Curmi PMG]] |
| - | [[Category: Littler, D R]] | + | [[Category: Harrop SJ]] |
| - | [[Category: Chloride ion channel]] | + | [[Category: Littler DR]] |
| - | [[Category: Clic]]
| + | |
| - | [[Category: Exc-4]]
| + | |
| - | [[Category: Gst fold]]
| + | |
| - | [[Category: Metal transport]]
| + | |
| Structural highlights
Function
EXC4_CAEEL May insert into membranes and form chloride ion channels. Involved in the formation of the excretory canal. Required to prevent cystic lumenal expansions in the excretory cell. Not required for formation of the initial tube, but is required for regulating the size of the tube lumen as it grows.[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 PubMed
The crystal structures of two CLIC family members DmCLIC and EXC-4 from the invertebrates Drosophila melanogaster and Caenorhabditis elegans, respectively, have been determined. The proteins adopt a glutathione S-transferase (GST) fold. The structures are highly homologous to each other and more closely related to the known structures of the human CLIC1 and CLIC4 than to GSTs. The invertebrate CLICs show several unique features including an elongated C-terminal extension and a divalent metal binding site. The latter appears to alter the ancestral glutathione binding site, and thus, the invertebrate CLICs are unlikely to bind glutathione in the same manner as the GST proteins. Purified recombinant DmCLIC and EXC-4 both bind to lipid bilayers and can form ion channels in artificial lipid bilayers, albeit at low pH. EXC-4 differs from other CLIC proteins in that the conserved redox-active cysteine at the N-terminus of helix 1 is replaced by an aspartic acid residue. Other key distinguishing features of EXC-4 include the fact that it binds to artificial bilayers at neutral pH and this binding is not sensitive to oxidation. These differences with other CLIC family members are likely to be due to the substitution of the conserved cysteine by aspartic acid. Proteins 2008. (c) 2007 Wiley-Liss, Inc.
Comparison of vertebrate and invertebrate CLIC proteins: The crystal structures of Caenorhabditis elegans EXC-4 and Drosophila melanogaster DmCLIC.,Littler DR, Harrop SJ, Brown LJ, Pankhurst GJ, Mynott AV, Luciani P, Mandyam RA, Mazzanti M, Tanda S, Berryman MA, Breit SN, Curmi PM Proteins. 2007 Oct 23;71(1):364-378. PMID:17985355[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Littler DR, Harrop SJ, Brown LJ, Pankhurst GJ, Mynott AV, Luciani P, Mandyam RA, Mazzanti M, Tanda S, Berryman MA, Breit SN, Curmi PM. Comparison of vertebrate and invertebrate CLIC proteins: The crystal structures of Caenorhabditis elegans EXC-4 and Drosophila melanogaster DmCLIC. Proteins. 2007 Oct 23;71(1):364-378. PMID:17985355 doi:10.1002/prot.21704
- ↑ Littler DR, Harrop SJ, Brown LJ, Pankhurst GJ, Mynott AV, Luciani P, Mandyam RA, Mazzanti M, Tanda S, Berryman MA, Breit SN, Curmi PM. Comparison of vertebrate and invertebrate CLIC proteins: The crystal structures of Caenorhabditis elegans EXC-4 and Drosophila melanogaster DmCLIC. Proteins. 2007 Oct 23;71(1):364-378. PMID:17985355 doi:10.1002/prot.21704
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