+Open data
-Basic information
Entry | Database: PDB / ID: 7q8b | |||||||||
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Title | Leishmania major actin filament in ADP-Pi state | |||||||||
Components | Actin | |||||||||
Keywords | STRUCTURAL PROTEIN / Actin / Filament / Parasite / ADP-Pi | |||||||||
Function / homology | Function and homology information kinetoplast / endonuclease activity / cytoskeleton / chromatin remodeling Similarity search - Function | |||||||||
Biological species | Leishmania major (eukaryote) | |||||||||
Method | ELECTRON MICROSCOPY / helical reconstruction / cryo EM / Resolution: 3.3 Å | |||||||||
Authors | Kotila, T. / Muniyandi, S. / Lappalainen, P. / Huiskonen, J.T. | |||||||||
Funding support | Finland, 2items
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Citation | Journal: Nat Commun / Year: 2022 Title: Structural basis of rapid actin dynamics in the evolutionarily divergent Leishmania parasite. Authors: Tommi Kotila / Hugo Wioland / Muniyandi Selvaraj / Konstantin Kogan / Lina Antenucci / Antoine Jégou / Juha T Huiskonen / Guillaume Romet-Lemonne / Pekka Lappalainen / Abstract: 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, ...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. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 7q8b.cif.gz | 326.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7q8b.ent.gz | 264.8 KB | Display | PDB format |
PDBx/mmJSON format | 7q8b.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/q8/7q8b ftp://data.pdbj.org/pub/pdb/validation_reports/q8/7q8b | HTTPS FTP |
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-Related structure data
Related structure data | 13863MC 7q8cC 7q8sC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments:
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