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Journal Article

Emergence of fractal geometries in the evolution of a metabolic enzyme

MPS-Authors
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Sendker,  Franziska Luisa
Max Planck Research Group Evolutionary Biochemistry, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Paczia,  Nicole       
Core Facility Metabolomics and small Molecules Mass Spectrometry, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

del Carmen Sánchez Olmos,  María
Core Facility MPG MAXGenesys DNAfoundry, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

/persons/resource/persons261244

Schindler,  Daniel       
Core Facility MPG MAXGenesys DNAfoundry, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

/persons/resource/persons254247

Erb,  Tobias J.       
Understanding and Building Metabolism, Department of Biochemistry and Synthetic Metabolism, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Bange,  Gert       
Max Planck Fellow Molecular Physiology of Microbes, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;
external;

/persons/resource/persons261248

Hochberg,  Georg K. A.       
Max Planck Research Group Evolutionary Biochemistry, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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https://doi.org/10.1038/s41586-024-07287-2
(Publisher version)

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Citation

Sendker, F. L., Lo, Y. K., Heimerl, T., Bohn, S., Persson, L. J., Mais, C.-N., et al. (2024). Emergence of fractal geometries in the evolution of a metabolic enzyme. Nature, 628(8009), 894-900. doi:10.1038/s41586-024-07287-2.


Cite as: https://hdl.handle.net/21.11116/0000-000F-23BD-5
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 Sierpiński 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.