Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

5OF2

The structural versatility of TasA in B. subtilis biofilm formation

Summary for 5OF2
Entry DOI10.2210/pdb5of2/pdb
DescriptorSpore coat-associated protein N, 1,2-ETHANEDIOL, SULFATE ION, ... (4 entities in total)
Functional Keywordstasa, biofilm matrix, amyloid fiber, xray structure, protein fibril
Biological sourceBacillus subtilis (strain 168)
Cellular locationSecreted : P54507
Total number of polymer chains1
Total formula weight23254.96
Authors
Primary citationDiehl, 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: 29531041
DOI: 10.1073/pnas.1718102115
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.86 Å)
Structure validation

247536

PDB entries from 2026-01-14

PDB statisticsPDBj update infoContact PDBjnumon