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Calixarene capture of partially unfolded cytochrome c
Author(s) -
Engilberge Sylvain,
Rennie Martin L.,
Crowley Peter B.
Publication year - 2019
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13512
Subject(s) - calixarene , supramolecular chemistry , chemistry , imidazole , cytochrome c , cytochrome , crystallography , stereochemistry , crystal structure , molecule , biochemistry , organic chemistry , enzyme , mitochondrion
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 ( sclx 6 ) and yeast cytochrome c (cyt c ) in the presence of imidazole. A crystal structure at 2.65 Å resolution reveals major structural rearrangement and disorder in imidazole‐bound cyt c . The largest protein‐calixarene interface involves 440 Å 2 of the protein surface with key contacts at Arg13, Lys73, and Lys79. These lysines participate in alkaline transitions of cyt c and are part of Ω‐loop D, which is substantially restructured in the complex with sclx 6 . The structural modification also includes Ω‐loop C, which is disordered (residues 41–55 inclusive). These results suggest the possibility of using supramolecular scaffolds to trap partially disordered proteins.