EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	Folding of an Intrinsically Disordered Iron-Binding Peptide in Response to Sedimentation Revealed by Cryo-EM.
ジャーナル・号・ページ	J Am Chem Soc, Vol. 142, Issue 46, Page 19551-19557, Year 2020
掲載日	2020年11月18日
著者	Geula Davidov / Gili Abelya / Ran Zalk / Benjamin Izbicki / Sharon Shaibi / Lior Spektor / Dayana Shagidov / Esther G Meyron-Holtz / Raz Zarivach / Gabriel A Frank /
PubMed 要旨	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. ...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.
リンク	J Am Chem Soc / PubMed:33166133 / PubMed Central
手法	EM (単粒子) / X線回折
解像度	1.7 - 3.5 Å
構造データ	11214 6zh5 EMDB-11214, PDB-6zh5: Folding of an iron binding peptide in response to sedimentation is resolved using ferritin as a nano-reactor 手法: EM (単粒子) / 解像度: 2.7 Å 11265 6zlg EMDB-11265, PDB-6zlg: Folding of an iron binding peptide in response to sedimentation is resolved using ferritin as a nano-reactor 手法: EM (単粒子) / 解像度: 3.0 Å 11272 6zlq EMDB-11272, PDB-6zlq: Folding of an iron binding peptide in response to sedimentation is resolved using ferritin as a nano-reactor 手法: EM (単粒子) / 解像度: 3.3 Å EMDB-11304: radiation damage-assisted analysis of iron-filled ferritin-M6A. 手法: EM (単粒子) / 解像度: 3.5 Å EMDB-11365: M6A and sediment structure inside iron-filled ferritin-M6A without symmetry assumption 手法: EM (単粒子) / 解像度: 3.1 Å PDB-6z3d: L-FerritinMSA 手法: X-RAY DIFFRACTION / 解像度: 1.7 Å
化合物	ChemComp-ACT: ACETATE ION / 酢酸イオン ChemComp-HOH: WATER ChemComp-FE: Unknown entry
由来	mus musculus (ハツカネズミ)
キーワード	METAL BINDING PROTEIN / Ferritin Iron storage protein / Biomineralization / nano-reactor / radiation damage assisted single-particle analysis