5of2: Difference between revisions
Jump to navigation
Jump to search
m Protected "5of2" [edit=sysop:move=sysop] |
No edit summary |
||
| (2 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
The | ==The structural versatility of TasA in B. subtilis biofilm formation== | ||
<StructureSection load='5of2' size='340' side='right'caption='[[5of2]], [[Resolution|resolution]] 1.86Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5of2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OF2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OF2 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.86Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5of2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5of2 OCA], [https://pdbe.org/5of2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5of2 RCSB], [https://www.ebi.ac.uk/pdbsum/5of2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5of2 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/TASA_BACSU 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).<ref>PMID:10049401</ref> <ref>PMID:10368135</ref> <ref>PMID:16430696</ref> <ref>PMID:20080671</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:29531041</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5of2" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
[[Category: | *[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]] | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Bacillus subtilis subsp. subtilis str. 168]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Akbey U]] | ||
[[Category: | [[Category: Ball L]] | ||
[[Category: | [[Category: Chowdhury A]] | ||
[[Category: | [[Category: Cremer N]] | ||
[[Category: | [[Category: Diehl A]] | ||
[[Category: | [[Category: Eisenmenger F]] | ||
[[Category: | [[Category: Heinemann U]] | ||
[[Category: | [[Category: Hiller M]] | ||
[[Category: | [[Category: Kramer R]] | ||
[[Category: Worth | [[Category: Leidert M]] | ||
[[Category: Lopez D]] | |||
[[Category: Moliere N]] | |||
[[Category: Nagaraj M]] | |||
[[Category: Oschkinat H]] | |||
[[Category: Roske Y]] | |||
[[Category: Schlegel B]] | |||
[[Category: Schmieder P]] | |||
[[Category: Stoeppler D]] | |||
[[Category: Turgay K]] | |||
[[Category: Worth CL]] | |||
Latest revision as of 19:47, 13 December 2023
The structural versatility of TasA in B. subtilis biofilm formationThe structural versatility of TasA in B. subtilis biofilm formation
Structural highlights
FunctionTASA_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 PubMedMicroorganisms 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 AlsoReferences
|
| ||||||||||||||||||