|Entry||Database: PDB / ID: 8aur|
|Title||Cryo-EM structure of a TasA fibre|
|Components||Major biofilm matrix component|
|Keywords||PROTEIN FIBRIL / Biofilm matrix fibre|
|Function / homology||Peptidase M73, camelysin / Camelysin metallo-endopeptidase / Signal peptide, camelysin / sporulation resulting in formation of a cellular spore / extracellular region / identical protein binding / Major biofilm matrix component|
Function and homology information
|Biological species||Bacillus subtilis (bacteria)|
|Method||ELECTRON MICROSCOPY / helical reconstruction / cryo EM / Resolution: 3.47 Å|
|Authors||Boehning, J. / Bharat, T.A.M.|
|Funding support|| United Kingdom, 1items |
Journal: Nat Commun / Year: 2022
Title: Donor-strand exchange drives assembly of the TasA scaffold in Bacillus subtilis biofilms.
Authors: Jan Böhning / Mnar Ghrayeb / Conrado Pedebos / Daniel K Abbas / Syma Khalid / Liraz Chai / Tanmay A M Bharat /
Abstract: Many bacteria in nature exist in multicellular communities termed biofilms, where cells are embedded in an extracellular matrix that provides rigidity to the biofilm and protects cells from chemical ...Many bacteria in nature exist in multicellular communities termed biofilms, where cells are embedded in an extracellular matrix that provides rigidity to the biofilm and protects cells from chemical and mechanical stresses. In the Gram-positive model bacterium Bacillus subtilis, TasA is the major protein component of the biofilm matrix, where it has been reported to form functional amyloid fibres contributing to biofilm structure and stability. Here, we present electron cryomicroscopy structures of TasA fibres, which show that, rather than forming amyloid fibrils, TasA monomers assemble into fibres through donor-strand exchange, with each subunit donating a β-strand to complete the fold of the next subunit along the fibre. Combining electron cryotomography, atomic force microscopy, and mutational studies, we show how TasA fibres congregate in three dimensions to form abundant fibre bundles that are essential for B. subtilis biofilm formation. Our study explains the previously observed biochemical properties of TasA and shows how a bacterial extracellular globular protein can assemble from monomers into β-sheet-rich fibres, and how such fibres assemble into bundles in biofilms.
|Structure viewer||Molecule: |
Downloads & links
A: Major biofilm matrix component
B: Major biofilm matrix component
C: Major biofilm matrix component
Mass: 25767.654 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Bacillus subtilis (bacteria) / Strain: 168 / References: UniProt: P54507
|Experiment||Method: ELECTRON MICROSCOPY|
|EM experiment||Aggregation state: FILAMENT / 3D reconstruction method: helical reconstruction|
|Component||Name: Three-subunit TasA filament / Type: COMPLEX / Entity ID: all / Source: NATURAL|
|Molecular weight||Value: 0.077211 MDa / Experimental value: NO|
|Source (natural)||Organism: Bacillus subtilis (bacteria) / Strain: ZK4363|
|Buffer solution||pH: 8|
|Specimen||Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES|
|Specimen support||Grid material: COPPER/RHODIUM / Grid mesh size: 200 divisions/in. / Grid type: Quantifoil R2/2|
|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 / Nominal defocus max: 2000 nm / Nominal defocus min: 1000 nm / Cs: 2.7 mm / Alignment procedure: ZEMLIN TABLEAU|
|Specimen holder||Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER|
|Image recording||Electron dose: 48.5 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k)|
|Software||Name: PHENIX / Version: 1.19.2_4158: / Classification: refinement|
|CTF correction||Type: PHASE FLIPPING AND AMPLITUDE CORRECTION|
|Helical symmerty||Angular rotation/subunit: -55.18 ° / Axial rise/subunit: 48.36 Å / Axial symmetry: C1|
|3D reconstruction||Resolution: 3.47 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 103009 / Symmetry type: HELICAL|
|Atomic model building||Protocol: AB INITIO MODEL / Space: REAL|
|Refine LS restraints|
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