Calixarene capture of partially unfolded cytochrome c

FEBS Letters

article

Sylvain Engilberge¹  Martin L. Rennie¹  Peter B. Crowley¹ 

[1] School of Chemistry, National University of Ireland Galway

关键词: disordered;    imidazole;    lysine;    omega loop;    supramolecular;   

DOI  :  10.1002/1873-3468.13512

来源: John Wiley & Sons Ltd.

【 摘 要 】

Supramolecular receptors such as water-soluble calixarenes are in development as ‘molecular glues’ for protein assembly. Here, we obtained cocrystals of sulfonato-calix[6]arene (sclx6) and yeast cytochrome c (cytc) in the presence of imidazole. A crystal structure at 2.65 A resolution reveals major structural rearrangement and disorder in imidazole-bound cytc. The largest protein-calixarene interface involves 440 A2 of the protein surface with key contacts at Arg13, Lys73, and Lys79. These lysines participate in alkaline transitions of cytc and are part of Ω-loop D, which is substantially restructured in the complex with sclx6. The structural modification also includes Ωloop C, which is disordered (residues 41–55 inclusive). These results suggest the possibility of using supramolecular scaffolds to trap partially disordered proteins.

【 授权许可】

Unknown