9BJO

Cryo-EM of Azo-ffsy fiber

これはPDB形式変換不可エントリーです。

9BJO の概要

• エントリーDOI: 10.2210/pdb9bjo/pdb
• EMDBエントリー: 44637
• 分子名称: D-peptide ffsy (1 entity in total)
• 機能のキーワード: d-peptide, peptide-fiber, helical, protein fibril
• 由来する生物種: synthetic construct
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 770.83

構造登録者

Zia, A.,Guo, J.,Xu, B.,Wang, F. (登録日: 2024-04-25, 公開日: 2024-09-18, 最終更新日: 2024-10-23)

主引用文献

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

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: 39255453
DOI: 10.1021/jacs.4c06775

実験手法

ELECTRON MICROSCOPY (2.8 Å)