Journal Article

PUBDB-2024-01718

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png 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. ; 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. (Corresponding author) ; Hochberg, G. K. A. (Corresponding author)

2024
Nature Publ. Group London [u.a.]

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Please use a persistent id in citations: doi:10.1038/s41586-024-07287-2  doi:10.3204/PUBDB-2024-01718

Abstract: Fractals are patterns that are self-similar across multiple length-scales1. Macroscopic fractals are common in nature2,3,4; however, so far, molecular assembly into fractals is restricted to synthetic systems5,6,7,8,9,10,11,12. 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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Contributing Institute(s):

1. EMBL-User (EMBL-User)

Research Program(s):

1. 6G3 - PETRA III (DESY) (POF4-6G3) (POF4-6G3)

Experiment(s):

1. PETRA Beamline P13 (PETRA III)

Appears in the scientific report 2024

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