Emergence of fractal geometries in the evolution of a metabolic enzyme

Sendker, Franziska Luisa; Lo, Yat Kei; Heimerl, Thomas; Bohn, Stefan; Persson, Louise J.; Mais, Christopher-Nils; Sadowska, Wiktoria; Paczia, Nicole; Nußbaum, Eva; del Carmen Sánchez Olmos, María; Forchhammer, Karl; Schindler, Daniel; Erb, Tobias J.; Benesch, Justin L. P.; Marklund, Erik G.; Bange, Gert; Schuller, Jan M.; Hochberg, Georg K. A.

doi:10.1038/s41586-024-07287-2

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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;

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

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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;

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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
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引用

Sendker, F. L., Lo, Y. K., Heimerl, T., Bohn, S., Persson, L. J., Mais, C.-N., Sadowska, W., Paczia, N., Nußbaum, E., del Carmen Sánchez Olmos, M., Forchhammer, K., Schindler, D., Erb, T. J., Benesch, J. L. P., Marklund, E. G., Bange, G., Schuller, J. M., & Hochberg, G. K. A. (2024). Emergence of fractal geometries in the evolution of a metabolic enzyme. Nature. doi:10.1038/s41586-024-07287-2.

引用: https://hdl.handle.net/21.11116/0000-000F-23BD-5

要旨

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.