View source for 4liz


==Crystal structure of coactosin from Entamoeba histolytica==
<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 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='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 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='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>
</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/>
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</StructureSection>
[[Category: Entamoeba histolytica HM-1:IMSS-A]]
[[Category: Large Structures]]
[[Category: Gourinath S]]
[[Category: Kumar N]]