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TitleStimulus-responsive self-assembly of protein-based fractals by computational design.
Journal, issue, pagesNat Chem, Vol. 11, Issue 7, Page 605-614, Year 2019
Publish dateJun 17, 2019
AuthorsNancy 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 /
PubMed AbstractFractal 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.
External linksNat Chem / PubMed:31209296
MethodsEM (tomography)
Structure data

EMDB-20062:
Fractal-like assemblies of designed AtzA and AtzC proteins
Method: EM (tomography)

EMDB-20063:
Fractal-like assemblies of designed AtzA and AtzC proteins
Method: EM (tomography)

Source
  • Pseudomonas sp. (bacteria)

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