6RGI

Partially unfolded cytochrome c in complex with sulfonatocalix[6]arene

Summary for 6RGI

• Entry DOI: 10.2210/pdb6rgi/pdb
• Descriptor: Cytochrome c iso-1, HEME C, p-sulfonatocalix[6]arene, ... (5 entities in total)
• Functional Keywords: molecular glues, calixarene, protein assembly, supramolecular chemistry, electron transport
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
• Total number of polymer chains: 1
• Total formula weight: 13840.42

Authors

Engilberge, S.,Rennie, M.L.,Crowley, P.B. (deposition date: 2019-04-16, release date: 2019-07-10, Last modification date: 2024-11-06)

Primary citation

Engilberge, S.,Rennie, M.L.,Crowley, P.B.
Calixarene capture of partially unfolded cytochrome c.
Febs Lett., 593:2112-2117, 2019

PubMed 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 ) and yeast cytochrome c (cytc) in the presence of imidazole. A crystal structure at 2.65 Å resolution reveals major structural rearrangement and disorder in imidazole-bound cytc. The largest protein-calixarene interface involves 440 Å 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 sclx . 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.

PubMed: 31254353
DOI: 10.1002/1873-3468.13512

Experimental method

X-RAY DIFFRACTION (2.64 Å)