7Q8C
Leishmania major actin filament in ADP-state
Summary for 7Q8C
Entry DOI | 10.2210/pdb7q8c/pdb |
Related | 7Q8B |
EMDB information | 13863 13864 |
Descriptor | Actin, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total) |
Functional Keywords | actin, filament, parasite, adp-pi, structural protein |
Biological source | Leishmania major |
Total number of polymer chains | 5 |
Total formula weight | 212576.86 |
Authors | Kotila, T.,Muniyandi, S.,Lappalainen, P.,Huiskonen, J.T. (deposition date: 2021-11-11, release date: 2022-05-18, Last modification date: 2024-07-17) |
Primary citation | Kotila, T.,Wioland, H.,Selvaraj, M.,Kogan, K.,Antenucci, L.,Jegou, A.,Huiskonen, J.T.,Romet-Lemonne, G.,Lappalainen, P. Structural basis of rapid actin dynamics in the evolutionarily divergent Leishmania parasite. Nat Commun, 13:3442-3442, 2022 Cited by PubMed 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, 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. PubMed: 35705539DOI: 10.1038/s41467-022-31068-y PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (2.72 Å) |
Structure validation
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