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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.*

Emergence of fractal geometries in the evolution of a metabolic enzyme.

Nature 628, 894-900 (2024)
Verlagsversion DOI PMC
Open Access Gold (Paid Option)
Creative Commons Lizenzvertrag
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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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Korrespondenzautor
Schlagwörter Cryo-em; Citrate Synthase; Phylogenetic Analysis; Sierpinski Triangles; Algorithms; Symmetry; Muscle; Forms
ISSN (print) / ISBN 0028-0836
e-ISSN 1476-4687
Zeitschrift Nature
Quellenangaben Band: 628, Heft: 8009, Seiten: 894-900 Artikelnummer: , Supplement: ,
Verlag Nature Publishing Group
Verlagsort London
Nichtpatentliteratur Publikationen
Begutachtungsstatus Peer reviewed
Institut(e) Institute of Structural Biology (STB)
Förderungen ERC
European Union
International Max Planck Research School for Principles of Microbial Life
DFG
Leverhulme Trust
Swedish Research Council
Helmholtz Association
Max Planck Society