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| <StructureSection load='7q8c' size='340' side='right'caption='[[7q8c]], [[Resolution|resolution]] 2.72Å' scene=''> | | <StructureSection load='7q8c' size='340' side='right'caption='[[7q8c]], [[Resolution|resolution]] 2.72Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[7q8c]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Q8C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Q8C FirstGlance]. <br> | | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Q8C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Q8C FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.72Å</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[7q8b|7q8b]]</div></td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=7q8c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7q8c OCA], [https://pdbe.org/7q8c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7q8c RCSB], [https://www.ebi.ac.uk/pdbsum/7q8c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7q8c 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=7q8c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7q8c OCA], [https://pdbe.org/7q8c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7q8c RCSB], [https://www.ebi.ac.uk/pdbsum/7q8c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7q8c ProSAT]</span></td></tr> |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
| |
| == Publication Abstract from PubMed ==
| |
| Actin polymerization generates forces for cellular processes throughout the eukaryotic kingdom, but our understanding of the 'ancient' actin turnover machineries is limited. We show that, despite > 1 billion years of evolution, pathogenic Leishmania major parasite and mammalian actins share the same overall fold and co-polymerize with each other. Interestingly, Leishmania harbors a simple actin-regulatory machinery that lacks cofilin 'cofactors', which accelerate filament disassembly in higher eukaryotes. By applying single-filament biochemistry we discovered that, compared to mammalian proteins, Leishmania actin filaments depolymerize more rapidly from both ends, and are severed > 100-fold more efficiently by cofilin. Our high-resolution cryo-EM structures of Leishmania ADP-, ADP-Pi- and cofilin-actin filaments identify specific features at actin subunit interfaces and cofilin-actin interactions that explain the unusually rapid dynamics of parasite actin filaments. Our findings reveal how divergent parasites achieve rapid actin dynamics using a remarkably simple set of actin-binding proteins, and elucidate evolution of the actin cytoskeleton.
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| Structural basis of rapid actin dynamics in the evolutionarily divergent Leishmania parasite.,Kotila T, Wioland H, Selvaraj M, Kogan K, Antenucci L, Jegou A, Huiskonen JT, Romet-Lemonne G, Lappalainen P Nat Commun. 2022 Jun 15;13(1):3442. doi: 10.1038/s41467-022-31068-y. PMID:35705539<ref>PMID:35705539</ref>
| | ==See Also== |
| | | *[[Actin 3D structures|Actin 3D structures]] |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 7q8c" style="background-color:#fffaf0;"></div>
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| == References == | |
| <references/>
| |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Huiskonen, J T]] | | [[Category: Huiskonen JT]] |
| [[Category: Kotila, T]] | | [[Category: Kotila T]] |
| [[Category: Lappalainen, P]] | | [[Category: Lappalainen P]] |
| [[Category: Muniyandi, S]] | | [[Category: Muniyandi S]] |
| [[Category: Actin]]
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| [[Category: Adp-pi]]
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| [[Category: Filament]]
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| [[Category: Parasite]]
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| [[Category: Structural protein]]
| |