Calixarene capture of partially unfolded cytochrome c. Issue 16 (7th July 2019)

• Record Type: Journal Article
• Authors: Engilberge, Sylvain; Rennie, Martin L.; Crowley, Peter B.
• Is Part Of: FEBS letters. Volume 593:Issue 16(2019)
• Page Start: 2112
• Page End: 2117
• Publication Date: 2019-07-07
• Subjects: disordered -- imidazole -- lysine -- omega loop -- supramolecular; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1002/1873-3468.13512
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : 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 withsclx 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. Abstract :