Summary for 9BJO
| Entry DOI | 10.2210/pdb9bjo/pdb |
| EMDB information | 44637 |
| Descriptor | D-peptide ffsy (1 entity in total) |
| Functional Keywords | d-peptide, peptide-fiber, helical, protein fibril |
| Biological source | synthetic construct |
| Total number of polymer chains | 1 |
| Total formula weight | 770.83 |
| Authors | |
| Primary citation | Guo, J.,Zia, A.,Qiu, Q.,Norton, M.,Qiu, K.,Usuba, J.,Liu, Z.,Yi, M.,Rich-New, S.T.,Hagan, M.,Fraden, S.,Han, G.D.,Diao, J.,Wang, F.,Xu, B. Cell-Free Nonequilibrium Assembly for Hierarchical Protein/Peptide Nanopillars. J.Am.Chem.Soc., 146:26102-26112, 2024 Cited by PubMed Abstract: 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. PubMed: 39255453DOI: 10.1021/jacs.4c06775 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.8 Å) |
Structure validation
Download full validation report
