7OO9

Structure of Chloroflexus islandicus LOV domain C85A variant (CisFbFP)

7OO9 の概要

• エントリーDOI: 10.2210/pdb7oo9/pdb
• 分子名称: Hybrid sensor histidine kinase/response regulator, FLAVIN MONONUCLEOTIDE, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: flavin, fluorescent protein
• 由来する生物種: Chloroflexus islandicus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 26947.88

構造登録者

Gushchin, I.,Remeeva, A.,Goncharov, I.M. (登録日: 2021-05-26, 公開日: 2021-06-30, 最終更新日: 2024-01-31)

主引用文献

Goncharov, I.M.,Smolentseva, A.,Semenov, O.,Natarov, I.,Nazarenko, V.V.,Yudenko, A.,Remeeva, A.,Gushchin, I.
High-resolution structure of a naturally red-shifted LOV domain.
Biochem.Biophys.Res.Commun., 567:143-147, 2021

PubMed Abstract: LOV domains are widespread photosensory modules that have also found applications in fluorescence microscopy, optogenetics, and light-driven generation of reactive oxygen species. Many of these applications require stable proteins with altered spectra. Here, we report a flavin-based fluorescent protein CisFbFP derived from Chloroflexus islandicus LOV domain-containing protein. We show that CisFbFP is thermostable, and its absorption and fluorescence spectra are red-shifted for ∼6 nm, which has not been observed for other cysteine-substituted natural LOV domains. We also provide a crystallographic structure of CisFbFP at the resolution of 1.2 Å that reveals alterations in the active site due to replacement of conservative asparagine with a serine. Finally, we discuss the possible effects of presence of cis-proline in the Aβ-Bβ loop on the protein's structure and stability. The findings provide the basis for engineering and color tuning of LOV-based tools for molecular biology.

PubMed: 34153684
DOI: 10.1016/j.bbrc.2021.06.046

実験手法

X-RAY DIFFRACTION (1.2 Å)