4bhu

From Proteopedia

(Difference between revisions)

Current revision

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 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 4bhu is ON HOLD
+==Crystal structure of BslA - A bacterial hydrophobin==
+<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_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='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='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/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 ==
+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.
-Authors: Rao, F.V., Hobley, L., Ostrowski, A., Bromley, K., Porter, M., Prescott, A., Swedlow, J.R., MacPhee, C., van Aalten, D.M.F., Stanley-Wall, N.R.
+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<ref>PMID:23904481</ref>
-Description: Crystal structure of BslA -A bacterial hydrophobin
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4bhu" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Bacillus subtilis subsp. subtilis NCIB 3610 = ATCC 6051 = DSM 10]]
+[[Category: Large Structures]]
+[[Category: Bromley KM]]
+[[Category: Hobley L]]
+[[Category: MacPhee CE]]
+[[Category: Ostrowski A]]
+[[Category: Porter M]]
+[[Category: Prescott AR]]
+[[Category: Rao FV]]
+[[Category: Stanley-Wall NR]]
+[[Category: Swedlow JR]]
+[[Category: Van Aalten DMF]]

4bhu

From Proteopedia

Current revision

Crystal structure of BslA - A bacterial hydrophobin

Structural highlights

Function

Publication Abstract from PubMed

References

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