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4bhu

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Crystal structure of BslA - A bacterial hydrophobin

Structural highlights

4bhu is a 10 chain structure with sequence from Bacillus subtilis subsp. subtilis NCIB 3610 = ATCC 6051 = DSM 10. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.91Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BSLA_BACSU Involved in biofilm formation (PubMed:18978066, PubMed:21742882). Self-polymerizes and forms a layer on the surface of biofilms that confers hydrophobicity to the biofilm (PubMed:22571672, PubMed:23904481). The layer is stable and capable of resistance to high mechanical force compression (PubMed:28701036). Required for complex colony architecture (PubMed:18978066). May function synergistically with exopolysaccharides and TasA amyloid fibers to facilitate the assembly of the biofilm matrix (PubMed:21742882).^[1] ^[2] ^[3] ^[4] ^[5]

Publication Abstract from PubMed

Biofilms represent the predominant mode of microbial growth in the natural environment. Bacillus subtilis is a ubiquitous Gram-positive soil bacterium that functions as an effective plant growth-promoting agent. The biofilm matrix is composed of an exopolysaccharide and an amyloid fiber-forming protein, TasA, and assembles with the aid of a small secreted protein, BslA. Here we show that natively synthesized and secreted BslA forms surface layers around the biofilm. Biophysical analysis demonstrates that BslA can self-assemble at interfaces, forming an elastic film. Molecular function is revealed from analysis of the crystal structure of BslA, which consists of an Ig-type fold with the addition of an unusual, extremely hydrophobic "cap" region. A combination of in vivo biofilm formation and in vitro biophysical analysis demonstrates that the central hydrophobic residues of the cap are essential to allow a hydrophobic, nonwetting biofilm to form as they control the surface activity of the BslA protein. The hydrophobic cap exhibits physiochemical properties remarkably similar to the hydrophobic surface found in fungal hydrophobins; thus, BslA is a structurally defined bacterial hydrophobin. We suggest that biofilms formed by other species of bacteria may have evolved similar mechanisms to provide protection to the resident bacterial community.

BslA is a self-assembling bacterial hydrophobin that coats the Bacillus subtilis biofilm.,Hobley L, Ostrowski A, Rao FV, Bromley KM, Porter M, Prescott AR, Macphee CE, van Aalten DM, Stanley-Wall NR Proc Natl Acad Sci U S A. 2013 Jul 31. PMID:23904481^[6]

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

References

↑ Verhamme DT, Murray EJ, Stanley-Wall NR. DegU and Spo0A jointly control transcription of two loci required for complex colony development by Bacillus subtilis. J Bacteriol. 2009 Jan;191(1):100-8. PMID:18978066 doi:10.1128/JB.01236-08
↑ Ostrowski A, Mehert A, Prescott A, Kiley TB, Stanley-Wall NR. YuaB functions synergistically with the exopolysaccharide and TasA amyloid fibers to allow biofilm formation by Bacillus subtilis. J Bacteriol. 2011 Sep;193(18):4821-31. PMID:21742882 doi:10.1128/JB.00223-11
↑ Kobayashi K, Iwano M. BslA(YuaB) forms a hydrophobic layer on the surface of Bacillus subtilis biofilms. Mol Microbiol. 2012 Jul;85(1):51-66. PMID:22571672 doi:10.1111/j.1365-2958.2012.08094.x
↑ Hobley L, Ostrowski A, Rao FV, Bromley KM, Porter M, Prescott AR, Macphee CE, van Aalten DM, Stanley-Wall NR. BslA is a self-assembling bacterial hydrophobin that coats the Bacillus subtilis biofilm. Proc Natl Acad Sci U S A. 2013 Jul 31. PMID:23904481 doi:10.1073/pnas.1306390110
↑ Liu W, Li S, Wang Z, Yan ECY, Leblanc RM. Characterization of Surface-Active Biofilm Protein BslA in Self-Assembling Langmuir Monolayer at the Air-Water Interface. Langmuir. 2017 Aug 1;33(30):7548-7555. PMID:28701036 doi:10.1021/acs.langmuir.7b01739
↑ Hobley L, Ostrowski A, Rao FV, Bromley KM, Porter M, Prescott AR, Macphee CE, van Aalten DM, Stanley-Wall NR. BslA is a self-assembling bacterial hydrophobin that coats the Bacillus subtilis biofilm. Proc Natl Acad Sci U S A. 2013 Jul 31. PMID:23904481 doi:10.1073/pnas.1306390110

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4bhu"

@@ Line 3: / Line 3: @@
 <StructureSection load='4bhu' size='340' side='right'caption='[[4bhu]], [[Resolution|resolution]] 1.91&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4bhu]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._atcc_6051 Bacillus subtilis subsp. subtilis str. atcc 6051]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BHU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BHU FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4bhu]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_NCIB_3610_=_ATCC_6051_=_DSM_10 Bacillus subtilis subsp. subtilis NCIB 3610 = ATCC 6051 = DSM 10]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BHU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BHU FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.91&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=4bhu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bhu OCA], [https://pdbe.org/4bhu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bhu RCSB], [https://www.ebi.ac.uk/pdbsum/4bhu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bhu ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/YUAB_BACSU YUAB_BACSU]] Required for complex colony architecture.
+[https://www.uniprot.org/uniprot/BSLA_BACSU BSLA_BACSU] Involved in biofilm formation (PubMed:18978066, PubMed:21742882). Self-polymerizes and forms a layer on the surface of biofilms that confers hydrophobicity to the biofilm (PubMed:22571672, PubMed:23904481). The layer is stable and capable of resistance to high mechanical force compression (PubMed:28701036). Required for complex colony architecture (PubMed:18978066). May function synergistically with exopolysaccharides and TasA amyloid fibers to facilitate the assembly of the biofilm matrix (PubMed:21742882).<ref>PMID:18978066</ref> <ref>PMID:21742882</ref> <ref>PMID:22571672</ref> <ref>PMID:23904481</ref> <ref>PMID:28701036</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus subtilis subsp. subtilis str. atcc 6051]]
+[[Category: Bacillus subtilis subsp. subtilis NCIB 3610 = ATCC 6051 = DSM 10]]
 [[Category: Large Structures]]
-[[Category: Aalten, D M.F van]]
+[[Category: Bromley KM]]
-[[Category: Bromley, K M]]
+[[Category: Hobley L]]
-[[Category: Hobley, L]]
+[[Category: MacPhee CE]]
-[[Category: MacPhee, C E]]
+[[Category: Ostrowski A]]
-[[Category: Ostrowski, A]]
+[[Category: Porter M]]
-[[Category: Porter, M]]
+[[Category: Prescott AR]]
-[[Category: Prescott, A R]]
+[[Category: Rao FV]]
-[[Category: Rao, F V]]
+[[Category: Stanley-Wall NR]]
-[[Category: Stanley-Wall, N R]]
+[[Category: Swedlow JR]]
-[[Category: Swedlow, J R]]
+[[Category: Van Aalten DMF]]
-[[Category: Biofilm]]
-[[Category: Structural protein]]

4bhu

From Proteopedia

Current revision

Crystal structure of BslA - A bacterial hydrophobin

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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