Emergence of fractal geometries in the evolution of a metabolic enzyme.
Nature
; 628(8009): 894-900, 2024 Apr.
Article
in En
| MEDLINE
| ID: mdl-38600380
ABSTRACT
Fractals are patterns that are self-similar across multiple length-scales1. Macroscopic fractals are common in nature2-4; however, so far, molecular assembly into fractals is restricted to synthetic systems5-12. Here we report the discovery of a natural protein, citrate synthase from the cyanobacterium Synechococcus elongatus, which self-assembles into Sierpinski triangles. Using cryo-electron microscopy, we reveal how the fractal assembles from a hexameric building block. Although different stimuli modulate the formation of fractal complexes and these complexes can regulate the enzymatic activity of citrate synthase in vitro, the fractal may not serve a physiological function in vivo. We use ancestral sequence reconstruction to retrace how the citrate synthase fractal evolved from non-fractal precursors, and the results suggest it may have emerged as a harmless evolutionary accident. Our findings expand the space of possible protein complexes and demonstrate that intricate and regulatable assemblies can evolve in a single substitution.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Citrate (si)-Synthase
/
Fractals
/
Evolution, Molecular
/
Synechococcus
/
Protein Multimerization
Language:
En
Journal:
Nature
/
Nature (Lond.)
/
Nature (London)
Year:
2024
Document type:
Article
Affiliation country:
Country of publication: