|Entry||Database: PDB / ID: 6izv|
|Title||Averaged strand structure of a 15-stranded ParM filament from Clostridium botulinum|
|Components||Putative plasmid segregation protein ParM|
|Keywords||PROTEIN FIBRIL / ParM / filaments / cytoskeleton|
|Function / homology||Actin-like protein, N-terminal / ParM-like / Actin like proteins N terminal domain / Uncharacterized protein|
Function and homology information
|Biological species||Clostridium botulinum Prevot_594 (bacteria)|
|Method||ELECTRON MICROSCOPY / helical reconstruction / cryo EM / Resolution: 4.2 Å|
|Authors||Koh, F. / Narita, A. / Lee, L.J. / Tan, Y.Z. / Dandey, V.P. / Tanaka, K. / Popp, D. / Robinson, R.C.|
|Funding support||United States , 3件 |
|Citation||Journal: Nat Commun / Year: 2019|
Title: The structure of a 15-stranded actin-like filament from Clostridium botulinum.
Authors: Fujiet Koh / Akihiro Narita / Lin Jie Lee / Kotaro Tanaka / Yong Zi Tan / Venkata P Dandey / David Popp / Robert C Robinson /
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 ...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.
SummaryFull reportAbout validation report
|Date||Deposition: Dec 20, 2018 / Release: Jun 19, 2019|
|Structure viewer||Molecule: |
Downloads & links
0: Putative plasmid segregation protein ParM
1: Putative plasmid segregation protein ParM
Mass: 39560.168 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Clostridium botulinum Prevot_594 (bacteria)
Gene: T258_3831 / Production host: Escherichia coli (E. coli) / References: UniProt: A0A0B4W229
Mass: 427.201 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Adenosine diphosphate / Comment: ADP (energy-carrying molecule) *YM
|Experiment||Method: ELECTRON MICROSCOPY|
|EM experiment||Aggregation state: FILAMENT / 3D reconstruction method: helical reconstruction|
|Component||Name: ParM filament coded on pCBH plasmid from Clostridium botulinum|
Type: COMPLEX / Entity ID: 1 / Source: RECOMBINANT
|Molecular weight||Experimental value: NO|
|Source (natural)||Organism: Clostridium botulinum F str. 230613 (bacteria) / Organelle: pCBH plasmid|
|Source (recombinant)||Organism: Escherichia coli BL21(DE3) (bacteria) / Plasmid: pET-21d|
|Buffer solution||pH: 7.4|
|Specimen||Conc.: 0.8 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES|
|Vitrification||Cryogen name: ETHANE|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Microscopy||Model: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM|
|Electron lens||Mode: BRIGHT FIELDBright-field microscopy|
|Image recording||Electron dose: 30 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k)|
|EM software||Name: RELION / Version: 2.1 / Category: 3D reconstruction|
|CTF correction||Type: PHASE FLIPPING AND AMPLITUDE CORRECTION|
|Helical symmerty||Angular rotation/subunit: -50.37 ° / Axial rise/subunit: 50.26 Å / Axial symmetry: C1|
|3D reconstruction||Resolution: 4.2 Å / Resolution method: OTHER / Num. of particles: 33356 / Symmetry type: HELICAL|
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