4bhu: Difference between revisions
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<StructureSection load='4bhu' size='340' side='right'caption='[[4bhu]], [[Resolution|resolution]] 1.91Å' scene=''> | <StructureSection load='4bhu' size='340' side='right'caption='[[4bhu]], [[Resolution|resolution]] 1.91Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4bhu]] is a 10 chain structure with sequence from [ | <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> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | </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> | ||
<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='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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <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> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/YUAB_BACSU YUAB_BACSU]] Required for complex colony architecture. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == |
Latest revision as of 10:14, 31 August 2022
Crystal structure of BslA - A bacterial hydrophobinCrystal structure of BslA - A bacterial hydrophobin
Structural highlights
Function[YUAB_BACSU] Required for complex colony architecture. Publication Abstract from PubMedBiofilms 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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