Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Folding of an Intrinsically Disordered Iron-Binding Peptide in Response to Sedimentation Revealed by Cryo-EM.
Journal, issue, pages	J Am Chem Soc, Vol. 142, Issue 46, Page 19551-19557, Year 2020
Publish date	Nov 18, 2020
Authors	Geula Davidov / Gili Abelya / Ran Zalk / Benjamin Izbicki / Sharon Shaibi / Lior Spektor / Dayana Shagidov / Esther G Meyron-Holtz / Raz Zarivach / Gabriel A Frank /
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. ...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.
External links	J Am Chem Soc / PubMed:33166133 / PubMed Central
Methods	EM (single particle) / X-ray diffraction
Resolution	1.7 - 3.5 Å
Structure data	11214 6zh5 EMDB-11214, PDB-6zh5: Folding of an iron binding peptide in response to sedimentation is resolved using ferritin as a nano-reactor Method: EM (single particle) / Resolution: 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 Method: EM (single particle) / Resolution: 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 Method: EM (single particle) / Resolution: 3.3 Å EMDB-11304: radiation damage-assisted analysis of iron-filled ferritin-M6A. Method: EM (single particle) / Resolution: 3.5 Å EMDB-11365: M6A and sediment structure inside iron-filled ferritin-M6A without symmetry assumption Method: EM (single particle) / Resolution: 3.1 Å PDB-6z3d: L-FerritinMSA Method: X-RAY DIFFRACTION / Resolution: 1.7 Å
Chemicals	ChemComp-ACT: ACETATE ION ChemComp-HOH: WATER ChemComp-FE: Unknown entry
Source	mus musculus (house mouse)
Keywords	METAL BINDING PROTEIN / Ferritin Iron storage protein / Biomineralization / nano-reactor / radiation damage assisted single-particle analysis