7q8c: Difference between revisions
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==Leishmania major actin filament in ADP-state== | ==Leishmania major actin filament in ADP-state== | ||
<StructureSection load='7q8c' size='340' side='right'caption='[[7q8c]]' scene=''> | <StructureSection load='7q8c' size='340' side='right'caption='[[7q8c]], [[Resolution|resolution]] 2.72Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<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> | <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> | ||
</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> | </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='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='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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7q8c" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Huiskonen | [[Category: Huiskonen, J T]] | ||
[[Category: Kotila T]] | [[Category: Kotila, T]] | ||
[[Category: Lappalainen P]] | [[Category: Lappalainen, P]] | ||
[[Category: Muniyandi S]] | [[Category: Muniyandi, S]] | ||
[[Category: Actin]] | |||
[[Category: Adp-pi]] | |||
[[Category: Filament]] | |||
[[Category: Parasite]] | |||
[[Category: Structural protein]] | |||
Revision as of 10:33, 29 June 2022
Leishmania major actin filament in ADP-stateLeishmania major actin filament in ADP-state
Structural highlights
Publication Abstract from PubMedActin 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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