6ZH5

Folding of an iron binding peptide in response to sedimentation is resolved using ferritin as a nano-reactor

6ZH5 の概要

• エントリーDOI: 10.2210/pdb6zh5/pdb
• 関連するPDBエントリー: 6Z3D
• EMDBエントリー: 11214
• 分子名称: Ferritin, FE (III) ION (2 entities in total)
• 機能のキーワード: biomineralization, nano-reactor, radiation damage assisted single-particle analysis, metal binding protein
• 由来する生物種: Mus musculus (House mouse)
• タンパク質・核酸の鎖数: 24
• 化学式量合計: 585583.34

構造登録者

Davidov, G.,Abelya, G.,Zalk, R.,Izbicki, B.,Shaibi, S.,Spektor, L.,Meyron Holtz, E.G.,Zarivach, R.,Frank, G.A. (登録日: 2020-06-21, 公開日: 2021-04-28, 最終更新日: 2025-07-09)

主引用文献

Davidov, G.,Abelya, G.,Zalk, R.,Izbicki, B.,Shaibi, S.,Spektor, L.,Shagidov, D.,Meyron-Holtz, E.G.,Zarivach, R.,Frank, G.A.
Folding of an Intrinsically Disordered Iron-Binding Peptide in Response to Sedimentation Revealed by Cryo-EM.
J.Am.Chem.Soc., 142:19551-19557, 2020

PubMed Abstract: Biomineralization is mediated by specialized proteins that guide and control mineral sedimentation. In many cases, the active regions of these biomineralization proteins are intrinsically disordered. High-resolution structures of these proteins while they interact with minerals are essential for understanding biomineralization processes and the function of intrinsically disordered proteins (IDPs). Here we used the cavity of ferritin as a nanoreactor where the interaction between M6A, an intrinsically disordered iron-binding domain, and an iron oxide particle was visualized at high resolution by cryo-EM. Taking advantage of the differences in the electron-dose sensitivity of the protein and the iron oxide particles, we developed a method to determine the irregular shape of the particles found in our density maps. We found that the folding of M6A correlates with the detection of mineral particles in its vicinity. M6A interacts with the iron oxide particles through its C-terminal side, resulting in the stabilization of a helix at its N-terminal side. The stabilization of the helix at a region that is not in direct contact with the iron oxide particle demonstrates the ability of IDPs to respond to signals from their surroundings by conformational changes. These findings provide the first glimpse toward the long-suspected mechanism for biomineralization protein control over mineral microstructure, where unstructured regions of these proteins become more ordered in response to their interaction with the nascent mineral particles.

PubMed: 33166133
DOI: 10.1021/jacs.0c07565

実験手法

ELECTRON MICROSCOPY (2.7 Å)