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Computational design of symmetrical eight-bladed beta-propeller proteins
- Source :
- IUCRJ, IUCrJ = International Union of Crystallography journal, IUCrJ = International Union of Crystallography journal, International Union of Crystallography 2019, 6 (1), pp.46-55. ⟨10.1107/S205225251801480X⟩, International Union of Crystallography journal, International Union of Crystallography journal, 2019, 6 (1), pp.46-55. ⟨10.1107/S205225251801480X⟩, IUCrJ 1 (6), 46-55. (2019), International Union of Crystallography journal, International Union of Crystallography 2019, 6 (1), pp.46-55. ⟨10.1107/S205225251801480X⟩, IUCrJ, IUCrJ, Vol 6, Iss 1, Pp 46-55 (2019)
- Publication Year :
- 2019
-
Abstract
- Two artificial β-propeller proteins with eight identical blades were designed, purified and crystallized. X-ray crystallography confirmed the perfectly symmetrical structures of these highly stable proteins.<br />β-Propeller proteins form one of the largest families of protein structures, with a pseudo-symmetrical fold made up of subdomains called blades. They are not only abundant but are also involved in a wide variety of cellular processes, often by acting as a platform for the assembly of protein complexes. WD40 proteins are a subfamily of propeller proteins with no intrinsic enzymatic activity, but their stable, modular architecture and versatile surface have allowed evolution to adapt them to many vital roles. By computationally reverse-engineering the duplication, fusion and diversification events in the evolutionary history of a WD40 protein, a perfectly symmetrical homologue called Tako8 was made. If two or four blades of Tako8 are expressed as single polypeptides, they do not self-assemble to complete the eight-bladed architecture, which may be owing to the closely spaced negative charges inside the ring. A different computational approach was employed to redesign Tako8 to create Ika8, a fourfold-symmetrical protein in which neighbouring blades carry compensating charges. Ika2 and Ika4, carrying two or four blades per subunit, respectively, were found to assemble spontaneously into a complete eight-bladed ring in solution. These artificial eight-bladed rings may find applications in bionanotechnology and as models to study the folding and evolution of WD40 proteins.
- Subjects :
- Subfamily
animal structures
Protein subunit
[SDV]Life Sciences [q-bio]
computational modelling
Molecular simulation
010402 general chemistry
01 natural sciences
Biochemistry
molecular simulation
β-propeller proteins
Beta-propeller
03 medical and health sciences
Protein structure
stomatognathic system
bioinformatics
protein structure
structural biology
WD40 proteins
Computational design
General Materials Science
030304 developmental biology
Physics
0303 health sciences
Crystallography
General Chemistry
Modular architecture
Condensed Matter Physics
Research Papers
0104 chemical sciences
Structural biology
QD901-999
Biological system
Subjects
Details
- Language :
- English
- ISSN :
- 20522525
- Database :
- OpenAIRE
- Journal :
- IUCRJ, IUCrJ = International Union of Crystallography journal, IUCrJ = International Union of Crystallography journal, International Union of Crystallography 2019, 6 (1), pp.46-55. ⟨10.1107/S205225251801480X⟩, International Union of Crystallography journal, International Union of Crystallography journal, 2019, 6 (1), pp.46-55. ⟨10.1107/S205225251801480X⟩, IUCrJ 1 (6), 46-55. (2019), International Union of Crystallography journal, International Union of Crystallography 2019, 6 (1), pp.46-55. ⟨10.1107/S205225251801480X⟩, IUCrJ, IUCrJ, Vol 6, Iss 1, Pp 46-55 (2019)
- Accession number :
- edsair.doi.dedup.....4b0954fdc23752d7e45b346ffae584fe