Computer Modeling of Structures of Reversibly Switchable Fluorescent Proteins with LOV Domains

The all-atom three-dimensional structures of novel reversibly switchable flavin-containing proteins with LOV (Light, Oxygen, Voltage) domains, used in ultrahigh-resolution microscopy, have been constructed for the first time using molecular modeling. Primary sequences (rather than spatial models) ar...

Full description

Saved in:
Bibliographic Details
Published in:Crystallography reports 2021-09, Vol.66 (5), p.815-818
Main Authors: Meteleshko, Yu. I., Khrenova, M. G., Nemukhin, A. V.
Format: Article
Language:English
Subjects:
Amino acids
Crystallography and Scattering Methods
Fluorescence
Modelling
Molecular dynamics
Mutation
Network analysis
Photoexcitation
Physics
Physics and Astronomy
Proteins
Signal transmission
Structure of Macromolecular Compounds
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The all-atom three-dimensional structures of novel reversibly switchable flavin-containing proteins with LOV (Light, Oxygen, Voltage) domains, used in ultrahigh-resolution microscopy, have been constructed for the first time using molecular modeling. Primary sequences (rather than spatial models) are known for the protein versions rsLOV1 and rsLOV2. The rsLOV1 and rsLOV2 models have been constructed based on the structure of a photoreceptor protein YtvA from Bacillus subtilis (Protein Data Bank (PDB) ID: 2MWG), with necessary point mutations of amino acid residues. The obtained models are solvated in water shells, and molecular dynamic trajectories are calculated and the dynamic network analysis is performed. It is shown that the dynamic properties of native and mutant structures differ primarily in regard of the Jα helix, which is responsible for signal transmission upon photoexcitation.
ISSN:1063-7745
1562-689X
DOI:10.1134/S106377452105014X