8ZBO

Crystal structure of the biphotochromic fluorescent protein moxSAASoti (F97M variant) in its green on-state

8ZBO の概要

• エントリーDOI: 10.2210/pdb8zbo/pdb
• 分子名称: F97M variant of the biphotochromic fluorescent protein moxSAASoti, NITRATE ION, 1,2-ETHANEDIOL, ... (5 entities in total)
• 機能のキーワード: moxsaasoti, point mutant, fluorescent protein, chromophore, msaasoti, saasoti, biphotochromic
• 由来する生物種: Stylocoeniella armata
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 51001.39

構造登録者

Boyko, K.M.,Matyuta, I.O.,Marynich, N.K.,Minyaev, M.E.,Khadiyatova, A.A.,Popov, V.O.,Savitsky, A.P. (登録日: 2024-04-26, 公開日: 2024-06-12, 最終更新日: 2026-03-18)

主引用文献

Marynich, N.K.,Boyko, K.M.,Matyuta, I.O.,Minyaev, M.E.,Khadiyatova, A.A.,Popov, V.O.,Savitsky, A.P.
Single-point substitution F97M leads to in cellulo crystallization of the biphotochromic protein moxSAASoti.
Biochem.Biophys.Res.Commun., 732:150419-150419, 2024

PubMed Abstract: To enhance the photoconversion performance of biphotochromic moxSAASoti protein, a substitution F97 M was introduced. In addition to enhancing the target properties, this substitution also resulted in the crystallization of the recombinant protein within living HeLa cells (also referred to as in cellulo crystallization). The phenomenon of protein crystallization in living cells is not unique, yet the mechanisms and application of in cellulo crystallization remain significant for further research. However, in cellulo crystallization is atypical for fluorescent proteins and detrimental for their biotechnological application. The objective of this study was to elucidate the underlying mechanisms responsible for the crystallization of moxSAASotiin cellulo. For this purpose, the crystal structure of the green form of biphotochromic protein moxSAASoti was determined at high resolution, which surprisingly has a space group, different from those of parent mSAASoti. The analysis provided allowed to propose a mechanism of new crystal contacts formation, which might be a cause of in cellulo protein crystallization.

PubMed: 39032411
DOI: 10.1016/j.bbrc.2024.150419

実験手法

X-RAY DIFFRACTION (2 Å)