Dataset for Spectroscopic, Structural and Dynamic Analysis of
Human Fe(II)/2OG-Dependent Dioxygenase ALKBH3
Научная публикация
| Журнал |
Data
|
| Вых. Данные |
Год: 2023,
Том: 8,
Номер статьи
: 57,
Страниц
:
DOI:
10.3390/data8030057
|
| Ключевые слова |
CD spectroscopy; fluorescent spectroscopy; dioxygenase; AlkB-like proteins; ALKBH3;
DNA methylation |
| Авторы |
Kanazhevskaya L.Y.
1
,
Gorbunov A.A.
2
,
Zhdanova P.V.
1
,
Koval V.V.
1,2
|
| Организации |
| 1 |
Institute of Chemical Biology and Fundamental Medicine SB RAS
|
| 2 |
Novosibirsk State University
|
|
Информация о финансировании (1)
|
1
|
Российский научный фонд
|
РНФ № 22-24-00699
|
Fe(II)/2OG-dependent dioxygenases of the AlkB family catalyze a direct removal of alkylated damages in the course of DNA and RNA repair. A human homolog of the E. coli AlkB ALKBH3
protein is able to hydroxylate N1-methyladenine, N3-methylcytosine, and N1-methylguanine in
single-stranded DNA and RNA. Due to its contribution to an antitumor drug resistance, this enzyme
is considered a promising therapeutic target. The elucidation of ALKBH3’s structural peculiarities
is important to establish a detailed mechanism of damaged DNA recognition and processing, as
well as to the development of specific inhibitors. This work presents new data on the wild type
ALKBH3 protein and its four mutant forms (Y143F, Y143A, L177A, and H191A) obtained by circular
dichroism (CD) spectroscopy. The dataset includes the CD spectra of proteins measured at different
temperatures and a 3D visualization of the ALKBH3–DNA complex where the mutated amino acid
residues are marked. These results show how substitution of the key amino acids influences a
secondary structure content of the protein.