5OF2
The structural versatility of TasA in B. subtilis biofilm formation
Summary for 5OF2
| Entry DOI | 10.2210/pdb5of2/pdb |
| Descriptor | Spore coat-associated protein N, 1,2-ETHANEDIOL, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | tasa, biofilm matrix, amyloid fiber, xray structure, protein fibril |
| Biological source | Bacillus subtilis (strain 168) |
| Cellular location | Secreted : P54507 |
| Total number of polymer chains | 1 |
| Total formula weight | 23254.96 |
| Authors | Roske, Y.,Diehl, A.,Ball, L.,Chowdhury, A.,Hiller, M.,Moliere, N.,Kramer, R.,Nagaraj, M.,Stoeppler, D.,Worth, C.L.,Schlegel, B.,Leidert, M.,Cremer, N.,Eisenmenger, F.,Lopez, D.,Schmieder, P.,Heinemann, U.,Turgay, K.,Akbey, U.,Oschkinat, H. (deposition date: 2017-07-10, release date: 2018-03-21, Last modification date: 2024-01-17) |
| Primary citation | Diehl, A.,Roske, Y.,Ball, L.,Chowdhury, A.,Hiller, M.,Moliere, N.,Kramer, R.,Stoppler, D.,Worth, C.L.,Schlegel, B.,Leidert, M.,Cremer, N.,Erdmann, N.,Lopez, D.,Stephanowitz, H.,Krause, E.,van Rossum, B.J.,Schmieder, P.,Heinemann, U.,Turgay, K.,Akbey, U.,Oschkinat, H. Structural changes of TasA in biofilm formation ofBacillus subtilis. Proc. Natl. Acad. Sci. U.S.A., 115:3237-3242, 2018 Cited by PubMed Abstract: Microorganisms form surface-attached communities, termed biofilms, which can serve as protection against host immune reactions or antibiotics. 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, β-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. PubMed: 29531041DOI: 10.1073/pnas.1718102115 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.86 Å) |
Structure validation
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