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- EMDB-20063: Fractal-like assemblies of designed AtzA and AtzC proteins -

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Basic information

Database: EMDB / ID: EMD-20063
TitleFractal-like assemblies of designed AtzA and AtzC proteins
Map data
SampleDesigned proteins AtzA-pY:AtzC-SH2Design
Biological speciesPseudomonas sp. (bacteria)
Methodelectron tomography / cryo EM
AuthorsDai W / Chen M / Khare S
CitationJournal: Nat Chem / Year: 2019
Title: Stimulus-responsive self-assembly of protein-based fractals by computational design.
Authors: Nancy E Hernández / William A Hansen / Denzel Zhu / Maria E Shea / Marium Khalid / Viacheslav Manichev / Matthew Putnins / Muyuan Chen / Anthony G Dodge / Lu Yang / Ileana Marrero-Berríos / Melissa Banal / Phillip Rechani / Torgny Gustafsson / Leonard C Feldman / Sang-Hyuk Lee / Lawrence P Wackett / Wei Dai / Sagar D Khare /
Abstract: Fractal topologies, which are statistically self-similar over multiple length scales, are pervasive in nature. The recurrence of patterns in fractal-shaped branched objects, such as trees, lungs and ...Fractal topologies, which are statistically self-similar over multiple length scales, are pervasive in nature. The recurrence of patterns in fractal-shaped branched objects, such as trees, lungs and sponges, results in a high surface area to volume ratio, which provides key functional advantages including molecular trapping and exchange. Mimicking these topologies in designed protein-based assemblies could provide access to functional biomaterials. Here we describe a computational design approach for the reversible self-assembly of proteins into tunable supramolecular fractal-like topologies in response to phosphorylation. Guided by atomic-resolution models, we develop fusions of Src homology 2 (SH2) domain or a phosphorylatable SH2-binding peptide, respectively, to two symmetric, homo-oligomeric proteins. Mixing the two designed components resulted in a variety of dendritic, hyperbranched and sponge-like topologies that are phosphorylation-dependent and self-similar over three decades (~10 nm-10 μm) of length scale, in agreement with models from multiscale computational simulations. Designed assemblies perform efficient phosphorylation-dependent capture and release of cargo proteins.
DateDeposition: Apr 5, 2019 / Header (metadata) release: May 1, 2019 / Map release: Jul 10, 2019 / Update: Jul 10, 2019

Structure visualization

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FileDownload / File: emd_20063.map.gz / Format: CCP4 / Size: 17.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

AxesZ (Sec.)Y (Row.)X (Col.)
27.9 Å/pix.
x 108 pix.
= 3013.2 Å
27.9 Å/pix.
x 170 pix.
= 4743. Å
27.9 Å/pix.
x 256 pix.
= 7142.4 Å


Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

generated in cubic-lattice coordinate

Voxel sizeX=Y=Z: 27.9 Å
Minimum - Maximum-3.9731262 - 3.9711313
Average (Standard dev.)-0.00027300356 (±0.71553123)
SymmetrySpace group: 1


Map geometry
Axis orderXYZ
CellA: 7142.4 Å / B: 4743.0 Å / C: 3013.2 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z27.927.927.9
M x/y/z256170108
origin x/y/z0.0000.0000.000
length x/y/z7142.4004743.0003013.200
MAP C/R/S123
start NC/NR/NS000
D min/max/mean-3.9733.971-0.000

Supplemental data

Sample components

Entire Designed proteins AtzA-pY:AtzC-SH2

EntireName: Designed proteins AtzA-pY:AtzC-SH2Design / Number of components: 1

Component #1: protein, Designed proteins AtzA-pY:AtzC-SH2

ProteinName: Designed proteins AtzA-pY:AtzC-SH2Design / Recombinant expression: No
SourceSpecies: Pseudomonas sp. (bacteria)
Source (engineered)Expression System: Escherichia coli (E. coli)

Experimental details

Sample preparation

SpecimenSpecimen state: Particle / Method: cryo EM
Sample solutionpH: 7
VitrificationInstrument: LEICA EM GP / Cryogen name: ETHANE / Temperature: 293 K / Humidity: 90 %

Electron microscopy imaging

Experimental equipment
Model: Talos Arctica / Image courtesy: FEI Company
ImagingMicroscope: FEI TECNAI ARCTICA
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Electron dose: 1 e/Å2 / Illumination mode: FLOOD BEAM
LensMagnification: 39000.0 X (nominal), 39000.0 X (calibrated) / Cs: 2.7 mm / Imaging mode: BRIGHT FIELD / Defocus: 4000.0 - 6000.0 nm / Energy filter: GIF Quantum LS
Specimen HolderModel: FEI TITAN KRIOS AUTOGRID HOLDER / Temperature: (93.0 - 110.0 K)
CameraDetector: GATAN K2 QUANTUM (4k x 4k)

Image processing

ProcessingMethod: electron tomography / Number of sections: 60
3D reconstructionAlgorithm: BACK PROJECTION / Software: EMAN2

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