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5of2

From Proteopedia

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The 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.

References

↑ 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
↑ 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
↑ 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
↑ 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
↑ 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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5of2"

@@ Line 1: / Line 1: @@
 ==The structural versatility of TasA in B. subtilis biofilm formation==
-<StructureSection load='5of2' size='340' side='right' caption='[[5of2]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
+<StructureSection load='5of2' size='340' side='right'caption='[[5of2]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5of2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacsu Bacsu]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OF2 FirstGlance]. <br>
+<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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.86&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tasA, cotN, yqhF, BSU24620 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5of2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5of2 OCA], [http://pdbe.org/5of2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5of2 RCSB], [http://www.ebi.ac.uk/pdbsum/5of2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5of2 ProSAT]</span></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 ==
@@ Line 17: / Line 19: @@
 </div>
 <div class="pdbe-citations 5of2" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Bacsu]]
+[[Category: Bacillus subtilis subsp. subtilis str. 168]]
-[[Category: Akbey, U]]
+[[Category: Large Structures]]
-[[Category: Ball, L]]
+[[Category: Akbey U]]
-[[Category: Chowdhury, A]]
+[[Category: Ball L]]
-[[Category: Cremer, N]]
+[[Category: Chowdhury A]]
-[[Category: Diehl, A]]
+[[Category: Cremer N]]
-[[Category: Eisenmenger, F]]
+[[Category: Diehl A]]
-[[Category: Heinemann, U]]
+[[Category: Eisenmenger F]]
-[[Category: Hiller, M]]
+[[Category: Heinemann U]]
-[[Category: Kramer, R]]
+[[Category: Hiller M]]
-[[Category: Leidert, M]]
+[[Category: Kramer R]]
-[[Category: Lopez, D]]
+[[Category: Leidert M]]
-[[Category: Moliere, N]]
+[[Category: Lopez D]]
-[[Category: Nagaraj, M]]
+[[Category: Moliere N]]
-[[Category: Oschkinat, H]]
+[[Category: Nagaraj M]]
-[[Category: Roske, Y]]
+[[Category: Oschkinat H]]
-[[Category: Schlegel, B]]
+[[Category: Roske Y]]
-[[Category: Schmieder, P]]
+[[Category: Schlegel B]]
-[[Category: Stoeppler, D]]
+[[Category: Schmieder P]]
-[[Category: Turgay, K]]
+[[Category: Stoeppler D]]
-[[Category: Worth, C L]]
+[[Category: Turgay K]]
-[[Category: Amyloid fiber]]
+[[Category: Worth CL]]
-[[Category: Biofilm matrix]]
-[[Category: Protein fibril]]
-[[Category: Tasa]]
-[[Category: Xray structure]]

5of2

From Proteopedia

Current revision

The structural versatility of TasA in B. subtilis biofilm formation

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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