8CF6

Dimethylated RSL-R5 in complex with cucurbit[7]uril, F432 cage assembly

8CF6 の概要

• エントリーDOI: 10.2210/pdb8cf6/pdb
• 分子名称: RSL-R5, methyl alpha-L-fucopyranoside, cucurbit[7]uril, ... (5 entities in total)
• 機能のキーワード: lectin, cucurbituril, biomaterials, supramolecular, sugar binding protein
• 由来する生物種: Ralstonia solanacearum
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 33021.18

構造登録者

Ramberg, K.,Crowley, P.B. (登録日: 2023-02-02, 公開日: 2023-07-05)

主引用文献

Ramberg, K.O.,Crowley, P.B.
Cage versus sheet: Probing the Determinants of Protein - Cucurbit[7]uril Crystalline Architectures.
J.Struct.Biol., 215:107969-107969, 2023

PubMed Abstract: The donut-shaped cucurbit[n]urils (Qn) are a class of rigid macrocyclic receptor with protein recognition capabilities. Qn encapsulation of amino acid side chains can enable protein assembly. Recently, cucurbit[7]uril (Q7) has been applied as a molecular glue for organizing protein building blocks into crystalline architectures. Q7 co-crystallization with dimethylated Ralstonia solanacearum lectin (RSL*) has yielded novel crystalline architectures. Co-crystallization of RSL* and Q7 yields either cage- or sheet-like architectures which may be modulated via protein engineering. However, questions remain as to the factors dictating the formation of one architecture over another (cage versus sheet). Here, we make use of an engineered RSL*-Q7 system which co-crystallizes as the cage or sheet assembly with easily-distinguished crystal morphologies. Using this model system, we probe how the crystallization conditions dictate which crystalline architecture is adopted. Protein-ligand ratios and the sodium concentration were identified as key determinants for the growth of the cage versus sheet assemblies.

PubMed: 37137399
DOI: 10.1016/j.jsb.2023.107969

実験手法

X-RAY DIFFRACTION (1.34 Å)