6IZR
Whole structure of a 15-stranded ParM filament from Clostridium botulinum
Summary for 6IZR
| Entry DOI | 10.2210/pdb6izr/pdb |
| EMDB information | 9757 |
| Descriptor | Putative plasmid segregation protein ParM, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION (3 entities in total) |
| Functional Keywords | parm, filaments, cytoskeleton, protein fibril |
| Biological source | Clostridium botulinum Prevot_594 |
| Total number of polymer chains | 30 |
| Total formula weight | 1200350.22 |
| Authors | Koh, F.,Narita, A.,Lee, L.J.,Tan, Y.Z.,Dandey, V.P.,Tanaka, K.,Popp, D.,Robinson, R.C. (deposition date: 2018-12-20, release date: 2019-06-19, Last modification date: 2024-05-29) |
| Primary citation | Koh, F.,Narita, A.,Lee, L.J.,Tanaka, K.,Tan, Y.Z.,Dandey, V.P.,Popp, D.,Robinson, R.C. The structure of a 15-stranded actin-like filament from Clostridium botulinum. Nat Commun, 10:2856-2856, 2019 Cited by PubMed Abstract: Microfilaments (actin) and microtubules represent the extremes in eukaryotic cytoskeleton cross-sectional dimensions, raising the question of whether filament architectures are limited by protein fold. Here, we report the cryoelectron microscopy structure of a complex filament formed from 15 protofilaments of an actin-like protein. This actin-like ParM is encoded on the large pCBH Clostridium botulinum plasmid. In cross-section, the ~26 nm diameter filament comprises a central helical protofilament surrounded by intermediate and outer layers of six and eight twisted protofilaments, respectively. Alternating polarity of the layers allows for similar lateral contacts between each layer. This filament design is stiffer than the actin filament, and has likely been selected for during evolution to move large cargos. The comparable sizes of microtubule and pCBH ParM filaments indicate that larger filament architectures are not limited by the protomer fold. Instead, function appears to have been the evolutionary driving force to produce broad, complex filaments. PubMed: 31253774DOI: 10.1038/s41467-019-10779-9 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.7 Å) |
Structure validation
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