4LIZ
Crystal structure of coactosin from Entamoeba histolytica
Summary for 4LIZ
| Entry DOI | 10.2210/pdb4liz/pdb |
| Related | 1T2l 1VFQ |
| Descriptor | Actin-binding protein, cofilin/tropomyosin family protein, putative, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, SODIUM ION, ... (4 entities in total) |
| Functional Keywords | coactosin, actin binding protein, actin, structural protein |
| Biological source | Entamoeba histolytica |
| Total number of polymer chains | 1 |
| Total formula weight | 16145.04 |
| Authors | Gourinath, S.,Kumar, N. (deposition date: 2013-07-04, release date: 2014-07-23, Last modification date: 2024-10-16) |
| Primary citation | Kumar, N.,Somlata,Mazumder, M.,Dutta, P.,Maiti, S.,Gourinath, S. EhCoactosin stabilizes actin filaments in the protist parasite Entamoeba histolytica. Plos Pathog., 10:e1004362-e1004362, 2014 Cited by PubMed Abstract: 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. PubMed: 25210743DOI: 10.1371/journal.ppat.1004362 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.499 Å) |
Structure validation
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