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  Emergence of fractal geometries in the evolution of a metabolic enzyme

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. doi:10.1038/s41586-024-07287-2.

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https://doi.org/10.1038/s41586-024-07287-2 (Verlagsversion)
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Sendker, Franziska Luisa1, Autor           
Lo, Yat Kei2, Autor
Heimerl, Thomas2, Autor
Bohn, Stefan2, Autor
Persson, Louise J.2, Autor
Mais, Christopher-Nils2, Autor
Sadowska, Wiktoria2, Autor
Paczia, Nicole3, Autor                 
Nußbaum, Eva2, Autor
del Carmen Sánchez Olmos, María4, Autor
Forchhammer, Karl2, Autor
Schindler, Daniel4, Autor                 
Erb, Tobias J.5, Autor                 
Benesch, Justin L. P.2, Autor
Marklund, Erik G.2, Autor
Bange, Gert2, 6, Autor                 
Schuller, Jan M.2, Autor
Hochberg, Georg K. A.1, Autor                 
Affiliations:
1Max Planck Research Group Evolutionary Biochemistry, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266300              
2external, ou_persistent22              
3Core Facility Metabolomics and small Molecules Mass Spectrometry, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266267              
4Core Facility MPG MAXGenesys DNAfoundry, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266268              
5Understanding and Building Metabolism, Department of Biochemistry and Synthetic Metabolism, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266303              
6Max Planck Fellow Molecular Physiology of Microbes, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3321791              

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 Zusammenfassung: 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.

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Sprache(n): eng - English
 Datum: 2024-04-10
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
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 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: URI: https://doi.org/10.1038/s41586-024-07287-2
Anderer: Sendker2024
DOI: 10.1038/s41586-024-07287-2
 Art des Abschluß: -

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Titel: Nature
  Kurztitel : Nature
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: London : Nature Publishing Group
Seiten: - Band / Heft: - Artikelnummer: - Start- / Endseite: - Identifikator: ISSN: 0028-0836
CoNE: https://pure.mpg.de/cone/journals/resource/954925427238