4liz: Difference between revisions

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 ==Crystal structure of coactosin from Entamoeba histolytica==
-<StructureSection load='4liz' size='340' side='right' caption='[[4liz]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
+<StructureSection load='4liz' size='340' side='right'caption='[[4liz]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4liz]] is a 1 chain structure. 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><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><br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.499&#8491;</td></tr>
-<tr><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='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><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1t2l|1t2l]], [[1vfq|1vfq]]</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><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://www.rcsb.org/pdb/explore.do?structureId=4liz RCSB], [http://www.ebi.ac.uk/pdbsum/4liz PDBsum]</span></td></tr>
+</table>
-<table>
+== Function ==
+[https://www.uniprot.org/uniprot/COAA_ENTH1 COAA_ENTH1] Actin-binding protein which is involved in F-actin stabilization (PubMed:25210743). May play a role during phagocytosis and pseudopod formation by contributing to the maintenance of F-actin (PubMed:25210743).<ref>PMID:25210743</ref>
+<div style="background-color:#fffaf0;">
+== 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<ref>PMID:25210743</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4liz" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>
-[[Category: Gourinath, S.]]
+[[Category: Entamoeba histolytica HM-1:IMSS-A]]
-[[Category: Kumar, N.]]
+[[Category: Large Structures]]
-[[Category: Actin]]
+[[Category: Gourinath S]]
-[[Category: Actin binding protein]]
+[[Category: Kumar N]]
-[[Category: Coactosin]]
-[[Category: Structural protein]]