8aur | pdb_00008aur

Cryo-EM structure of a TasA fibre

spinqualitylabelsall models 8aur, resolution 3.47Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8aur is a 3 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TASA_BACSU TasA is the major protein component of the biofilm extracellular matrix (PubMed:16430696, PubMed:20080671). It forms amyloid fibers that bind cells together in the biofilm (PubMed:20080671). Exhibits an antibacterial activity against a variety of Gram-positive and Gram-negative bacteria (PubMed:10049401). In laboratory strains, is also involved in proper spore coat assembly (PubMed:10368135). Publication Abstract from PubMed 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 beta-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 beta-sheet-rich fibres, and how such fibres assemble into bundles in biofilms. Donor-strand exchange drives assembly of the TasA scaffold in Bacillus subtilis biofilms.,Bohning J, Ghrayeb M, Pedebos C, Abbas DK, Khalid S, Chai L, Bharat TAM Nat Commun. 2022 Nov 18;13(1):7082. doi: 10.1038/s41467-022-34700-z. PMID:36400765 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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