5nl7: Difference between revisions
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<StructureSection load='5nl7' size='340' side='right'caption='[[5nl7]], [[Resolution|resolution]] 2.48Å' scene=''> | <StructureSection load='5nl7' size='340' side='right'caption='[[5nl7]], [[Resolution|resolution]] 2.48Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5nl7]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NL7 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5NL7 FirstGlance]. <br> | <table><tr><td colspan='2'>[[5nl7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Enthi Enthi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NL7 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5NL7 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CL6EHI_199000, EHI_199000 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5759 ENTHI])</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=5nl7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nl7 OCA], [http://pdbe.org/5nl7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nl7 RCSB], [http://www.ebi.ac.uk/pdbsum/5nl7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nl7 ProSAT]</span></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=5nl7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nl7 OCA], [http://pdbe.org/5nl7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nl7 RCSB], [http://www.ebi.ac.uk/pdbsum/5nl7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nl7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:32848067</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5nl7" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Enthi]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Djinovic-Carugo, K]] | [[Category: Djinovic-Carugo, K]] | ||
Revision as of 10:28, 4 November 2020
The crystal structure of the Actin Binding Domain (ABD) of alpha actinin from Entamoeba histolyticaThe crystal structure of the Actin Binding Domain (ABD) of alpha actinin from Entamoeba histolytica
Structural highlights
Publication Abstract from PubMedThe 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
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