Тип публикации: статья из журнала

Год издания: 2024

Идентификатор DOI: 10.3390/life14111508

Аннотация: <jats:p>Here, we describe (1) the AlphaFold-based structural modeling approach to identify amino acids of the photoprotein berovin that are crucial for coelenterazine binding, and (2) the production and characterization of berovin mutants with substitutions of the identified residues regarding their effects on the ability to form aПоказать полностьюn active photoprotein under physiological conditions and stability to light irradiation. The combination of mutations K90M, N107S, and W103F is demonstrated to cause a shift of optimal conditions for the conversion of apo-berovin into active photoprotein towards near-neutral pH and low ionic strength, and to reduce the sensitivity of active berovin to light. According to the berovin spatial structure model, these residues are found in close proximity to the 6-(p-hydroxy)-phenyl group of the coelenterazine peroxyanion.</jats:p>

Журнал: Life

Выпуск журнала: Т. 14, № 11

Номера страниц: 1508

ISSN журнала: 20751729

• Burakova Ludmila P. (Institute of Fundamental Biology and Biotechnology, Siberian Federal University, Krasnoyarsk 660041, Russia)
• Ivanisenko Nikita V. (AIRI, Moscow 123112, Russia)
• Rukosueva Natalia V. (Institute of Fundamental Biology and Biotechnology, Siberian Federal University, Krasnoyarsk 660041, Russia)
• Ivanisenko Vladimir A. (Novosibirsk State University, Novosibirsk 630090, Russia)
• Vysotski Eugene S. (Photobiology Laboratory, Institute of Biophysics of Siberian Branch of the Russian Academy of Sciences, Federal Research Center “Krasnoyarsk Science Center” of Siberian Branch of the Russian Academy of Sciences, Krasnoyarsk 660036, Russia)

• Ядро РИНЦ (eLIBRARY.RU)