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| | <StructureSection load='5nl6' size='340' side='right'caption='[[5nl6]], [[Resolution|resolution]] 2.05Å' scene=''> | | <StructureSection load='5nl6' size='340' side='right'caption='[[5nl6]], [[Resolution|resolution]] 2.05Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5nl6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Entamoeba_histolytica_hm-1:imss Entamoeba histolytica hm-1:imss]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NL6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5NL6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5nl6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Entamoeba_histolytica_HM-1:IMSS Entamoeba histolytica HM-1:IMSS]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NL6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NL6 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</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]] 2.05Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EHI7A_134780 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=294381 Entamoeba histolytica HM-1:IMSS])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5nl6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nl6 OCA], [http://pdbe.org/5nl6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nl6 RCSB], [http://www.ebi.ac.uk/pdbsum/5nl6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nl6 ProSAT]</span></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=5nl6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nl6 OCA], [https://pdbe.org/5nl6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nl6 RCSB], [https://www.ebi.ac.uk/pdbsum/5nl6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nl6 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/N9TIJ7_ENTH1 N9TIJ7_ENTH1] |
| | <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]] | + | [[Category: Entamoeba histolytica HM-1:IMSS]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Djinovic-Carugo, K]] | + | [[Category: Djinovic-Carugo K]] |
| - | [[Category: Khan, M B]] | + | [[Category: Khan MB]] |
| - | [[Category: Pinotsis, N]] | + | [[Category: Pinotsis N]] |
| - | [[Category: Actinin]]
| + | |
| - | [[Category: Entamoeba histolytica]]
| + | |
| - | [[Category: Spectrin repeat]]
| + | |
| - | [[Category: Structural protein]]
| + | |
| Structural highlights
Function
N9TIJ7_ENTH1
Publication Abstract from PubMed
The actin cytoskeleton, a dynamic network of actin filaments and associated F-actin-binding proteins, is fundamentally important in eukaryotes. alpha-Actinins are major F-actin bundlers that are inhibited by Ca(2+) in nonmuscle cells. Here we report the mechanism of Ca(2+)-mediated regulation of Entamoeba histolytica alpha-actinin-2 (EhActn2) with features expected for the common ancestor of Entamoeba and higher eukaryotic alpha-actinins. Crystal structures of Ca(2+)-free and Ca(2+)-bound EhActn2 reveal a calmodulin-like domain (CaMD) uniquely inserted within the rod domain. Integrative studies reveal an exceptionally high affinity of the EhActn2 CaMD for Ca(2+), binding of which can only be regulated in the presence of physiological concentrations of Mg(2+) Ca(2+) binding triggers an increase in protein multidomain rigidity, reducing conformational flexibility of F-actin-binding domains via interdomain cross-talk and consequently inhibiting F-actin bundling. In vivo studies uncover that EhActn2 plays an important role in phagocytic cup formation and might constitute a new drug target for amoebic dysentery.
Calcium modulates the domain flexibility and function of an alpha-actinin similar to the ancestral alpha-actinin.,Pinotsis N, Zielinska K, Babuta M, Arolas JL, Kostan J, Khan MB, Schreiner C, Salmazo A, Ciccarelli L, Puchinger M, Gkougkoulia EA, Ribeiro EA Jr, Marlovits TC, Bhattacharya A, Djinovic-Carugo K Proc Natl Acad Sci U S A. 2020 Sep 8;117(36):22101-22112. doi:, 10.1073/pnas.1917269117. Epub 2020 Aug 26. PMID:32848067[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pinotsis N, Zielinska K, Babuta M, Arolas JL, Kostan J, Khan MB, Schreiner C, Salmazo A, Ciccarelli L, Puchinger M, Gkougkoulia EA, Ribeiro EA Jr, Marlovits TC, Bhattacharya A, Djinovic-Carugo K. Calcium modulates the domain flexibility and function of an alpha-actinin similar to the ancestral alpha-actinin. Proc Natl Acad Sci U S A. 2020 Sep 8;117(36):22101-22112. doi:, 10.1073/pnas.1917269117. Epub 2020 Aug 26. PMID:32848067 doi:http://dx.doi.org/10.1073/pnas.1917269117
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