The structural versatility of TasA in B. subtilis biofilm formationThe structural versatility of TasA in B. subtilis biofilm formation

Structural highlights

5of2 is a 1 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 1.86Å
Ligands:,
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).[1] [2] [3] [4]

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[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Stover AG, Driks A. Secretion, localization, and antibacterial activity of TasA, a Bacillus subtilis spore-associated protein. J Bacteriol. 1999 Mar;181(5):1664-72. doi: 10.1128/JB.181.5.1664-1672.1999. PMID:10049401 doi:http://dx.doi.org/10.1128/JB.181.5.1664-1672.1999
  2. Serrano M, Zilhao R, Ricca E, Ozin AJ, Moran CP Jr, Henriques AO. A Bacillus subtilis secreted protein with a role in endospore coat assembly and function. J Bacteriol. 1999 Jun;181(12):3632-43. doi: 10.1128/JB.181.12.3632-3643.1999. PMID:10368135 doi:http://dx.doi.org/10.1128/JB.181.12.3632-3643.1999
  3. Branda SS, Chu F, Kearns DB, Losick R, Kolter R. A major protein component of the Bacillus subtilis biofilm matrix. Mol Microbiol. 2006 Feb;59(4):1229-38. doi: 10.1111/j.1365-2958.2005.05020.x. PMID:16430696 doi:http://dx.doi.org/10.1111/j.1365-2958.2005.05020.x
  4. Romero D, Aguilar C, Losick R, Kolter R. Amyloid fibers provide structural integrity to Bacillus subtilis biofilms. Proc Natl Acad Sci U S A. 2010 Feb 2;107(5):2230-4. doi: 10.1073/pnas.0910560107. , Epub 2010 Jan 13. PMID:20080671 doi:http://dx.doi.org/10.1073/pnas.0910560107
  5. 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. Structural changes of TasA in biofilm formation of Bacillus subtilis. Proc Natl Acad Sci U S A. 2018 Mar 12. pii: 1718102115. doi:, 10.1073/pnas.1718102115. PMID:29531041 doi:http://dx.doi.org/10.1073/pnas.1718102115

5of2, resolution 1.86Å

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