6S99

Dimethylated fusion protein of RSL and trimeric coiled coil in complex with cucurbit[7]uril

Summary for 6S99

• Entry DOI: 10.2210/pdb6s99/pdb
• Related: 6F37
• Descriptor: 4dzn-RSL,Fucose-binding lectin protein,Fucose-binding lectin protein, beta-D-mannopyranose, cucurbit[7]uril, ... (4 entities in total)
• Functional Keywords: fusion protein, molecular glues, crystal engineering, cucurbituril, sugar binding protein
• Biological source: Ralstonia solanacearum (Pseudomonas solanacearum); More
• Total number of polymer chains: 6
• Total formula weight: 83388.61

Authors

Ramberg, K.,Engilberge, S.,Crowley, P.B. (deposition date: 2019-07-11, release date: 2020-08-26, Last modification date: 2022-12-07)

Primary citation

Ramberg, K.O.,Guagnini, F.,Engilberge, S.,Wronska, M.A.,Rennie, M.L.,Perez, J.,Crowley, P.B.
Segregated Protein-Cucurbit[7]uril Crystalline Architectures via Modulatory Peptide Tectons.
Chemistry, 2021

PubMed Abstract: One approach to protein assembly involves water-soluble supramolecular receptors that act like glues. Bionanoarchitectures directed by these scaffolds are often system-specific, with few studies investigating their customization. Herein, the modulation of cucurbituril-mediated protein assemblies through the inclusion of peptide tectons is described. Three peptides of varying length and structural order were N-terminally appended to RSL, a β-propeller building block. Each fusion protein was incorporated into crystalline architectures mediated by cucurbit[7]uril (Q7). A trimeric coiled-coil served as a spacer within a Q7-directed sheet assembly of RSL, giving rise to a layered material of varying porosity. Within the spacer layers, the coiled-coils were dynamic. This result prompted consideration of intrinsically disordered peptides (IDPs) as modulatory tectons. Similar to the coiled-coil, a mussel adhesion peptide (Mefp) also acted as a spacer between protein-Q7 sheets. In contrast, the fusion of a nucleoporin peptide (Nup) to RSL did not recapitulate the sheet assembly. Instead, a Q7-directed cage was adopted, within which disordered Nup peptides were partially "captured" by Q7 receptors. IDP capture occurred by macrocycle recognition of an intrapeptide Phe-Gly motif in which the benzyl group was encapsulated by Q7. The modularity of these protein-cucurbituril architectures adds a new dimension to macrocycle-mediated protein assembly. Segregated protein crystals, with alternating layers of high and low porosity, could provide a basis for new types of materials.

PubMed: 34432924
DOI: 10.1002/chem.202103025

Experimental method

X-RAY DIFFRACTION (2.649 Å)