8AN1
Structure of a first level Sierpinski triangle formed by a citrate synthase
Summary for 8AN1
| Entry DOI | 10.2210/pdb8an1/pdb |
| EMDB information | 15529 |
| Descriptor | Citrate synthase (1 entity in total) |
| Functional Keywords | fractal complex, transferase |
| Biological source | Synechococcus elongatus PCC 7942 = FACHB-805 |
| Total number of polymer chains | 18 |
| Total formula weight | 798612.68 |
| Authors | Lo, Y.K.,Bohn, S.,Sendker, F.L.,Schuller, J.M.,Hochberg, G. (deposition date: 2022-08-04, release date: 2024-02-21, Last modification date: 2024-09-11) |
| Primary citation | Sendker, F.L.,Lo, Y.K.,Heimerl, T.,Bohn, S.,Persson, L.J.,Mais, C.N.,Sadowska, W.,Paczia, N.,Nussbaum, E.,Del Carmen Sanchez 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 Cited by PubMed Abstract: Fractals are patterns that are self-similar across multiple length-scales. Macroscopic fractals are common in nature; however, so far, molecular assembly into fractals is restricted to synthetic systems. 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. PubMed: 38600380DOI: 10.1038/s41586-024-07287-2 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.93 Å) |
Structure validation
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