Standard

Design of Ctenophore Ca2+-Regulated Photoprotein Berovin Capable of Being Converted into Active Protein Under Physiological Conditions: Computational and Experimental Approaches. / Burakova, Ludmila P.; Ivanisenko, Nikita V.; Rukosueva, Natalia V. и др.

в: Life, Том 14, № 11, 1508, 11.2024.

Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование

Harvard

Burakova, LP, Ivanisenko, NV, Rukosueva, NV, Ivanisenko, VA & Vysotski, ES 2024, 'Design of Ctenophore Ca2+-Regulated Photoprotein Berovin Capable of Being Converted into Active Protein Under Physiological Conditions: Computational and Experimental Approaches', Life, Том. 14, № 11, 1508. https://doi.org/10.3390/life14111508

APA

Burakova, L. P., Ivanisenko, N. V., Rukosueva, N. V., Ivanisenko, V. A., & Vysotski, E. S. (2024). Design of Ctenophore Ca2+-Regulated Photoprotein Berovin Capable of Being Converted into Active Protein Under Physiological Conditions: Computational and Experimental Approaches. Life, 14(11), [1508]. https://doi.org/10.3390/life14111508

Vancouver

Burakova LP, Ivanisenko NV, Rukosueva NV, Ivanisenko VA, Vysotski ES. Design of Ctenophore Ca2+-Regulated Photoprotein Berovin Capable of Being Converted into Active Protein Under Physiological Conditions: Computational and Experimental Approaches. Life. 2024 нояб.;14(11):1508. doi: 10.3390/life14111508

Author

Burakova, Ludmila P. ; Ivanisenko, Nikita V. ; Rukosueva, Natalia V. и др. / Design of Ctenophore Ca2+-Regulated Photoprotein Berovin Capable of Being Converted into Active Protein Under Physiological Conditions: Computational and Experimental Approaches. в: Life. 2024 ; Том 14, № 11.

BibTeX

@article{c8d845004d694b559606e82b0d9adb34,
title = "Design of Ctenophore Ca2+-Regulated Photoprotein Berovin Capable of Being Converted into Active Protein Under Physiological Conditions: Computational and Experimental Approaches",
abstract = "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 an 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.",
keywords = "AlphaFold, berovin, bioluminescence, coelenterazine, ctenophore, molecular modeling, photoprotein",
author = "Burakova, {Ludmila P.} and Ivanisenko, {Nikita V.} and Rukosueva, {Natalia V.} and Ivanisenko, {Vladimir A.} and Vysotski, {Eugene S.}",
note = "This research was funded by Russian Science Foundation, grant number 22-14-00125.",
year = "2024",
month = nov,
doi = "10.3390/life14111508",
language = "English",
volume = "14",
journal = "Life",
issn = "2075-1729",
publisher = "Multidisciplinary Digital Publishing Institute (MDPI)",
number = "11",

}

RIS

TY - JOUR

T1 - Design of Ctenophore Ca2+-Regulated Photoprotein Berovin Capable of Being Converted into Active Protein Under Physiological Conditions: Computational and Experimental Approaches

AU - Burakova, Ludmila P.

AU - Ivanisenko, Nikita V.

AU - Rukosueva, Natalia V.

AU - Ivanisenko, Vladimir A.

AU - Vysotski, Eugene S.

N1 - This research was funded by Russian Science Foundation, grant number 22-14-00125.

PY - 2024/11

Y1 - 2024/11

N2 - 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 an 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.

AB - 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 an 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.

KW - AlphaFold

KW - berovin

KW - bioluminescence

KW - coelenterazine

KW - ctenophore

KW - molecular modeling

KW - photoprotein

UR - https://www.scopus.com/record/display.uri?eid=2-s2.0-85210554121&origin=inward&txGid=fcc2ca370b114057cd75d11a8e0258e5

UR - https://www.mendeley.com/catalogue/77a864ab-dc30-31e3-a9fa-e693d13989af/

U2 - 10.3390/life14111508

DO - 10.3390/life14111508

M3 - Article

C2 - 39598306

VL - 14

JO - Life

JF - Life

SN - 2075-1729

IS - 11

M1 - 1508

ER -

ID: 61146866