7P2I

Dimethylated fusion protein of RSL and nucleoporin peptide (Nup) in complex with cucurbit[7]uril, F432 cage assembly

7P2I の概要

• エントリーDOI: 10.2210/pdb7p2i/pdb
• 関連するPDBエントリー: 6F37 6S99 7P2H
• 分子名称: Fucose-binding lectin protein, methyl alpha-L-fucopyranoside, cucurbit[7]uril, ... (4 entities in total)
• 機能のキーワード: biomaterials, coiled coil, crystal engineering, idp, macrocycle, sugar binding protein
• 由来する生物種: Ralstonia solanacearum (Pseudomonas solanacearum)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 36617.55

構造登録者

Guagnini, F.,Ramberg, K.,Crowley, P.B. (登録日: 2021-07-06, 公開日: 2021-09-08, 最終更新日: 2024-01-31)

主引用文献

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, 27:14619-14627, 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

実験手法

X-RAY DIFFRACTION (1.489 Å)