5of1

The structural versatility of TasA in B. subtilis biofilm formation

spinqualitylabelsall models 5of1, resolution 1.56Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5of1 is a 2 chain structure with sequence from Bacillus subtilis subsp. subtilis str. 168. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.56Å Ligands: EDO, MSE, SAL 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 Microorganisms form surface-attached communities, termed biofilms, which can serve as protection against host immune reactions or antibiotics. Bacillus subtilis biofilms contain TasA as major proteinaceous component in addition to exopolysaccharides. In stark contrast to the initially unfolded biofilm proteins of other bacteria, TasA is a soluble, stably folded monomer, whose structure we have determined by X-ray crystallography. Subsequently, we characterized in vitro different oligomeric forms of TasA by NMR, EM, X-ray diffraction, and analytical ultracentrifugation (AUC) experiments. However, by magic-angle spinning (MAS) NMR on live biofilms, a swift structural change toward only one of these forms, consisting of homogeneous and protease-resistant, beta-sheet-rich fibrils, was observed in vivo. Thereby, we characterize a structural change from a globular state to a fibrillar form in a functional prokaryotic system on the molecular level. Structural changes of TasA in biofilm formation of Bacillus subtilis.,Diehl A, Roske Y, Ball L, Chowdhury A, Hiller M, Moliere N, Kramer R, Stoppler D, Worth CL, Schlegel B, Leidert M, Cremer N, Erdmann N, Lopez D, Stephanowitz H, Krause E, van Rossum BJ, Schmieder P, Heinemann U, Turgay K, Akbey U, Oschkinat H Proc Natl Acad Sci U S A. 2018 Mar 12. pii: 1718102115. doi:, 10.1073/pnas.1718102115. PMID:29531041 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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