7q8s: Difference between revisions

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-'''Unreleased structure'''
-The entry 7q8s is ON HOLD
+==Leishmania major ADP-actin filament decorated with Leishmania major cofilin==
+<StructureSection load='7q8s' size='340' side='right'caption='[[7q8s]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[7q8s]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Leishmania_major Leishmania major]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Q8S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Q8S FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.4&#8491;</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=7q8s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7q8s OCA], [https://pdbe.org/7q8s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7q8s RCSB], [https://www.ebi.ac.uk/pdbsum/7q8s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7q8s ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ACT_LEIMA ACT_LEIMA] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
+<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 &gt; 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 &gt; 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.
-Authors:
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 7q8s" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Actin 3D structures|Actin 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Leishmania major]]
+[[Category: Huiskonen JT]]
+[[Category: Kotila T]]
+[[Category: Lappalainen P]]
+[[Category: Muniyandi S]]