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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)

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Fractals are patterns that are self-similar across multiple length-scales¹. Macroscopic fractals are common in nature^2-4; however, so far, molecular assembly into fractals is restricted to synthetic systems^5-12. 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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