Literature summary for 1.14.14.3 extracted from

Nemtseva, E.V.; Gulnov, D.V.; Gerasimova, M.A.; Sukovatyi, L.A.; Burakova, L.P.; Karuzina, N.E.; Melnik, B.S.; Kratasyuk, V.A.
Bacterial luciferases from Vibrio harveyi and Photobacterium leiognathi demonstrate different conformational stability as detected by time-resolved fluorescence spectroscopy (2021), Int. J. Mol. Sci., 22, 14994 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
comparison of the conformational transitions of luciferases from Vibrio harveyi and Photobacterium leiognathi during equilibrium unfolding with urea. Vibrio harveyi luciferase in its native state demonstrates a higher fluorescence intensity per one protein molecule, but a shorter fluorescence lifetime, than Photobacterium leiognathi luciferase. During the first stage of denaturation (at more than 2 M of urea), for V. harveyi luciferase, the fluorescence lifetimes tau1 and tau2 show an increase, while for the P. leiognathi enzyme, the lifetime components decrease. This stage includes the unfolding of the C-terminal domain of the luciferase alpha-subunit. Subunit dissociation does not influence the optical characteristics of either of the luciferases. The unfolding of the subunits occurs in the same way for the two proteins	Vibrio harveyi
comparison of the conformational transitions of luciferases from Vibrio harveyi and Photobacterium leiognathi during equilibrium unfolding with urea. Vibrio harveyi luciferase in its native state demonstrates a higher fluorescence intensity per one protein molecule, but a shorter fluorescence lifetime, than Photobacterium leiognathi luciferase. During the first stage of denaturation (at more than 2 M of urea), for V. harveyi luciferase, the fluorescence lifetimes tau1 and tau2 show an increase, while for the P. leiognathi enzyme, the lifetime components decrease. This stage includes the unfolding of the C-terminal domain of the luciferase alpha-subunit. Subunit dissociation does not influence the optical characteristics of either of the luciferases. The unfolding of the subunits occurs in the same way for the two proteins	Photobacterium leiognathi

Crystallization (Comment)

Organism

comparison of the conformational transitions of luciferases from Vibrio harveyi and Photobacterium leiognathi during equilibrium unfolding with urea. Vibrio harveyi luciferase in its native state demonstrates a higher fluorescence intensity per one protein molecule, but a shorter fluorescence lifetime, than Photobacterium leiognathi luciferase. During the first stage of denaturation (at more than 2 M of urea), for V. harveyi luciferase, the fluorescence lifetimes tau1 and tau2 show an increase, while for the P. leiognathi enzyme, the lifetime components decrease. This stage includes the unfolding of the C-terminal domain of the luciferase alpha-subunit. Subunit dissociation does not influence the optical characteristics of either of the luciferases. The unfolding of the subunits occurs in the same way for the two proteins

Vibrio harveyi

Photobacterium leiognathi

Organism

Organism	UniProt	Comment	Textmining
Photobacterium leiognathi	P09140 and P09141	P09140 i.e. alpha subunit LuxA, P09141 i.e. beta subunit LuxB	-
Vibrio harveyi	P07740 and P07739	P07740 i.e. subunit LuxA, P07739 i.e. subunit LuxB	-