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| | ==Crystal structure of coactosin from Entamoeba histolytica== | | ==Crystal structure of coactosin from Entamoeba histolytica== |
| - | <StructureSection load='4liz' size='340' side='right' caption='[[4liz]], [[Resolution|resolution]] 1.50Å' scene=''> | + | <StructureSection load='4liz' size='340' side='right'caption='[[4liz]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4liz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Entamoeba_histolytica_hm-1:imss-a Entamoeba histolytica hm-1:imss-a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LIZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LIZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4liz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Entamoeba_histolytica_HM-1:IMSS-A Entamoeba histolytica HM-1:IMSS-A]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LIZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LIZ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=4liz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4liz OCA], [https://pdbe.org/4liz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4liz RCSB], [https://www.ebi.ac.uk/pdbsum/4liz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4liz ProSAT]</span></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1t2l|1t2l]], [[1vfq|1vfq]]</td></tr>
| + | |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Actin binding protein, Cofilin/tropomyosin family, EHI7A_006660 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=885318 Entamoeba histolytica HM-1:IMSS-A])</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=4liz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4liz OCA], [http://pdbe.org/4liz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4liz RCSB], [http://www.ebi.ac.uk/pdbsum/4liz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4liz ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/N9TKD6_ENTHI N9TKD6_ENTHI] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Entamoeba histolytica hm-1:imss-a]] | + | [[Category: Entamoeba histolytica HM-1:IMSS-A]] |
| - | [[Category: Gourinath, S]] | + | [[Category: Large Structures]] |
| - | [[Category: Kumar, N]] | + | [[Category: Gourinath S]] |
| - | [[Category: Actin]] | + | [[Category: Kumar N]] |
| - | [[Category: Actin binding protein]]
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| - | [[Category: Coactosin]]
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| - | [[Category: Structural protein]]
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| Structural highlights
Function
N9TKD6_ENTHI
Publication Abstract from PubMed
Entamoeba histolytica is a protist parasite that is the causative agent of amoebiasis, and is a highly motile organism. The motility is essential for its survival and pathogenesis, and a dynamic actin cytoskeleton is required for this process. EhCoactosin, an actin-binding protein of the ADF/cofilin family, participates in actin dynamics, and here we report our studies of this protein using both structural and functional approaches. The X-ray crystal structure of EhCoactosin resembles that of human coactosin-like protein, with major differences in the distribution of surface charges and the orientation of terminal regions. According to in vitro binding assays, full-length EhCoactosin binds both F- and G-actin. Instead of acting to depolymerize or severe F-actin, EhCoactosin directly stabilizes the polymer. When EhCoactosin was visualized in E. histolytica cells using either confocal imaging or total internal reflectance microscopy, it was found to colocalize with F-actin at phagocytic cups. Over-expression of this protein stabilized F-actin and inhibited the phagocytic process. EhCoactosin appears to be an unusual type of coactosin involved in E. histolytica actin dynamics.
EhCoactosin stabilizes actin filaments in the protist parasite Entamoeba histolytica.,Kumar N, Somlata, Mazumder M, Dutta P, Maiti S, Gourinath S PLoS Pathog. 2014 Sep 11;10(9):e1004362. doi: 10.1371/journal.ppat.1004362., eCollection 2014 Sep. PMID:25210743[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kumar N, Somlata, Mazumder M, Dutta P, Maiti S, Gourinath S. EhCoactosin stabilizes actin filaments in the protist parasite Entamoeba histolytica. PLoS Pathog. 2014 Sep 11;10(9):e1004362. doi: 10.1371/journal.ppat.1004362., eCollection 2014 Sep. PMID:25210743 doi:http://dx.doi.org/10.1371/journal.ppat.1004362
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