7BBT

Structure of cytochrome c in complex with a p-benzyl-sulfonato-calix[8]arene-PEG pseudorotaxane

Summary for 7BBT

• Entry DOI: 10.2210/pdb7bbt/pdb
• Related: 6RSI
• Descriptor: Cytochrome c iso-1, HEME C, 4-[[49,50,51,52,53,54,55,56-octahydroxy-11,17,23,29,35,41,47-heptakis[(4-sulfonatophenyl)methyl]-5-nonacyclo[43.3.1.13,7.19,13.115,19.121,25.127,31.133,37.139,43]hexapentaconta-1(49),3,5,7(56),9,11,13(55),15,17,19(54),21,23,25(53),27,29,31(52),33,35,37(51),39,41,43(50),45,47-tetracosaenyl]methyl]benzenesulfonate, ... (5 entities in total)
• Functional Keywords: extended-arm, molecular recognition, biohybrid, alpha-helix, oxidoreductase
• Biological source: Saccharomyces cerevisiae S288C
• Total number of polymer chains: 4
• Total formula weight: 58778.12

Authors

Mockler, N.M.,Ramberg, K.,Guagnini, F.,Raston, C.L.,Crowley, P.B. (deposition date: 2020-12-18, release date: 2021-10-20, Last modification date: 2024-10-16)

Primary citation

Mockler, N.M.,Ramberg, K.O.,Guagnini, F.,Raston, C.L.,Crowley, P.B.
Noncovalent Protein-Pseudorotaxane Assembly Incorporating an Extended Arm Calix[8]arene with alpha-Helical Recognition Properties.
Cryst.Growth Des., 21:1424-1427, 2021

PubMed Abstract: Water-soluble, anionic calix[]arenes are useful receptors for protein recognition and assembly. For example, sulfonato-calix[8]arene ( ) can encapsulate proteins and direct their assembly into porous frameworks. In this work, we turned our attention to an "extended arm" calixarene with 16 phenyl rings. We hypothesized that this larger receptor would have increased capacity for protein masking/encapsulation. A cocrystal structure of -benzyl-sulfonato-calix[8]arene ( ) and cytochrome (cyt ) revealed a surprising assembly. A pseudorotaxane comprising a stack of three molecules threaded by polyethylene glycol (PEG) was bound to the protein. The trimeric stack, a tubelike structure with a highly charged surface, mediated assembly via a new mode of protein recognition. The calixarene stack presents four hydrophobic grooves, each of which binds to one cyt by accommodating the N-terminal α-helix. This unprecedented binding mode suggests new possibilities for supramolecular protein chemistry.

PubMed: 34054353
DOI: 10.1021/acs.cgd.0c01717

Experimental method

X-RAY DIFFRACTION (3.023 Å)