6GD7

Auto-regulated Protein Assembly on a Supramolecular Scaffold.

(2018) Angew Chem Int Ed Engl 57: 13764-13769

• PubMed: 30109907 Search on PubMed
• DOI: https://doi.org/10.1002/anie.201807490
• Primary Citation of Related Structures:  
  6GD6, 6GD7, 6GD8, 6GD9


• PubMed Abstract: 
  

  Controlled protein assembly provides a means to regulate function. Supramolecular building blocks, including rigid macrocycles, are versatile triggers of protein assembly. Now it is shown that sulfonato-calix[8]arene (sclx ₈ ) mediates the formation of cytochrome?c tetramers in solution. This tetramer spontaneously disassembles at ≥2?equivalents of sclx ₈ , providing a remarkable example of auto-regulation. Using X-ray crystallography the sclx ₈ binding sites on cytochrome?c were characterized. Crystal structures at different protein-ligand ratios reveal varying degrees (up to 35?%) of protein surface coverage by the flexible calixarene and suggest a mechanism for oligomer disassembly. The solution structure of the oligomer was characterized by small-angle X-ray scattering. Overall, the data indicate calixarene-controlled protein assembly and disassembly without the requirement for a competitive inhibitor, and point to protein encapsulation by a flexible macrocycle.

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Organizational Affiliation: 

School of Chemistry, National University of Ireland Galway, University Road, Galway, Ireland.