View source for 9bjo


==Cryo-EM of Azo-ffsy fiber==
<StructureSection load='9bjo' size='340' side='right'caption='[[9bjo]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9bjo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9BJO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9BJO FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A1APX:4-[(~{E})-phenyldiazenyl]benzoic+acid'>A1APX</scene>, <scene name='pdbligand=DPN:D-PHENYLALANINE'>DPN</scene>, <scene name='pdbligand=DSN:D-SERINE'>DSN</scene>, <scene name='pdbligand=DTY:D-TYROSINE'>DTY</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=9bjo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9bjo OCA], [https://pdbe.org/9bjo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9bjo RCSB], [https://www.ebi.ac.uk/pdbsum/9bjo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9bjo ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cells contain intricate protein nanostructures, but replicating them outside of cells presents challenges. One such example is the vertical fibronectin pillars observed in embryos. Here, we demonstrate the creation of cell-free vertical fibronectin pillar mimics using nonequilibrium self-assembly. Our approach utilizes enzyme-responsive phosphopeptides that assemble into nanotubes. Enzyme action triggers shape changes in peptide assemblies, driving the vertical growth of protein nanopillars into bundles. These bundles, with peptide nanotubes serving as a template to remodel fibronectin, can then recruit collagen, which forms aggregates or bundles depending on their types. Nanopillar formation relies on enzyme-catalyzed nonequilibrium self-assembly and is governed by the concentrations of enzyme, protein, peptide, the structure of the peptide, and peptide assembly morphologies. Cryo-EM reveals unexpected nanotube thinning and packing after dephosphorylation, indicating a complex sculpting process during assembly. Our study demonstrates a cell-free method for constructing intricate, multiprotein nanostructures with directionality and composition.

Cell-Free Nonequilibrium Assembly for Hierarchical Protein/Peptide Nanopillars.,Guo J, Zia A, Qiu Q, Norton M, Qiu K, Usuba J, Liu Z, Yi M, Rich-New ST, Hagan M, Fraden S, Han GD, Diao J, Wang F, Xu B J Am Chem Soc. 2024 Sep 10. doi: 10.1021/jacs.4c06775. PMID:39255453<ref>PMID:39255453</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9bjo" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Guo J]]
[[Category: Wang F]]
[[Category: Xu B]]
[[Category: Zia A]]