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8RJK

Pseudoatomic model of a second-order Sierpinski triangle formed by the citrate synthase from Synechococcus elongatus

Summary for 8RJK
Entry DOI10.2210/pdb8rjk/pdb
EMDB information19250
DescriptorCitrate synthase (1 entity in total)
Functional Keywordsfractal complex, transferase
Biological sourceSynechococcus elongatus PCC 7942 = FACHB-805
Total number of polymer chains54
Total formula weight2396866.79
Authors
Lo, Y.K.,Bohn, S.,Sendker, F.L.,Schuller, J.M.,Hochberg, G. (deposition date: 2023-12-21, release date: 2024-02-28, Last modification date: 2024-05-08)
Primary citationSendker, 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: 38600380
DOI: 10.1038/s41586-024-07287-2
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (5.91 Å)
Structure validation

226707

数据于2024-10-30公开中

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