7P8Y

Short wilavidin apo form

7P8Y の概要

• エントリーDOI: 10.2210/pdb7p8y/pdb
• 関連するPDBエントリー: 7OUQ 7OUR 7OUS
• 分子名称: Wilavidin, PENTAETHYLENE GLYCOL, HEXAETHYLENE GLYCOL, ... (6 entities in total)
• 機能のキーワード: biotin binding protein, avidin, biotechnology, unknown function
• 由来する生物種: Gammaproteobacteria bacterium
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 53963.27

構造登録者

Avraham, O.,Livnah, O. (登録日: 2021-07-23, 公開日: 2021-11-17, 最終更新日: 2024-10-16)

主引用文献

Avraham, O.,Bayer, E.A.,Livnah, O.
Wilavidin - a novel member of the avidin family that forms unique biotin-binding hexamers.
Febs J., 289:1700-1714, 2022

PubMed Abstract: Nature's optimization of protein functions is a highly intricate evolutionary process. In addition to optimal tertiary folding, the intramolecular recognition among the monomers that generate higher-order quaternary arrangements is driven by stabilizing interactions that have a pivotal role for ideal activity. Homotetrameric avidin and streptavidin are regularly utilized in many applications, whereby their ultra-high affinity toward biotin is dependent on their quaternary arrangements. In recent years, a new subfamily of avidins was discovered that comprises homodimers rather than tetramers, in which the high affinity toward biotin is maintained. Intriguingly, several of the respective dimers have been shown to assemble into higher-order cylindrical hexamers or octamers that dissociate into dimers upon biotin binding. Here, we present wilavidin, a newly discovered member of the dimeric subfamily, forming hexamers in the apo form, which are uniquely maintained upon biotin binding with six high-affinity binding sites. Removal of the short C-terminal segment of wilavidin resulted in the presence of the dimer only, thus emphasizing the role of this segment in stabilizing the hexamer. Utilization of a hexavalent biotin-binding form of avidin would be beneficial for expanding the biotechnological toolbox. Additionally, this unique family of dimeric avidins and their propensity to oligomerize to hexamers or octamers can serve as a basis for protein oligomerization and intermonomeric recognition as well as cumulative interactions that determine molecular assemblies.

PubMed: 34726340
DOI: 10.1111/febs.16259

実験手法

X-RAY DIFFRACTION (2.18 Å)