6GBA

A fast recovering full-length LOV protein (DsLOV) from the marine phototrophic bacterium Dinoroseobacter shibae (Dark state) - M49A mutant

6GBA の概要

• エントリーDOI: 10.2210/pdb6gba/pdb
• 分子名称: Putative blue-light photoreceptor, FLAVIN MONONUCLEOTIDE (3 entities in total)
• 機能のキーワード: light-oxygen-voltage, lov, pas, signaling protein
• 由来する生物種: Dinoroseobacter shibae (strain DSM 16493 / NCIMB 14021 / DFL 12)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17257.15

構造登録者

Granzin, J.,Batra-Safferling, R.,Roellen, K. (登録日: 2018-04-13, 公開日: 2018-07-18, 最終更新日: 2024-01-17)

主引用文献

Fettweiss, T.,Rollen, K.,Granzin, J.,Reiners, O.,Endres, S.,Drepper, T.,Willbold, D.,Jaeger, K.E.,Batra-Safferling, R.,Krauss, U.
Mechanistic Basis of the Fast Dark Recovery of the Short LOV Protein DsLOV from Dinoroseobacter shibae.
Biochemistry, 57:4833-4847, 2018

PubMed Abstract: Light, oxygen, voltage (LOV) proteins, a ubiquitously distributed class of photoreceptors, regulate a wide variety of light-dependent physiological responses. Because of their modular architecture, LOV domains, i.e., the sensory domains of LOV photoreceptors, have been widely used for the construction of optogenetic tools. We recently described the structure and function of a short LOV protein (DsLOV) from the marine phototropic bacterium Dinoroseobacter shibae, for which, in contrast to other LOV photoreceptors, the dark state represents the physiologically relevant signaling state. Among bacterial LOV photoreceptors, DsLOV possesses an exceptionally fast dark recovery, corroborating its function as a "dark" sensor. To address the mechanistic basis of this unusual characteristic, we performed a comprehensive mutational, kinetic, thermodynamic, and structural characterization of DsLOV. The mechanistic basis of the fast dark recovery of the protein was revealed by mutation of the previously noted uncommon residue substitution at position 49 found in DsLOV. The substitution of M49 with different residues that are naturally conserved in LOV domains tuned the dark-recovery time of DsLOV over 3 orders of magnitude, without grossly affecting its overall structure or the light-dependent structural change observed for the wild-type protein. Our study thus provides a striking example of how nature can achieve LOV photocycle tuning by subtle structural alterations in the LOV domain active site, highlighting the easy evolutionary adaptability of the light sensory function. At the same time, our data provide guidance for the mutational photocycle tuning of LOV domains, with relevance for the growing field of optogenetics.

PubMed: 29989797
DOI: 10.1021/acs.biochem.8b00645

実験手法

X-RAY DIFFRACTION (1.9 Å)