| Autor: |
Ziyuan Zhou, Qing Pan, Xinchen Lv, Jing Yuan, Yang Zhang, Ming-Xia Zhang, Ming Ke, Xiao-Mei Mo, Yong-Li Xie, Yingxia Liu, Ting Chen, Mingchan Liang, Feng Yin, Lei Liu, Yiqing Zhou, Kun Qiao, Rui Liu, Zigang Li, Nai-Kei Wong |
| Jazyk: |
angličtina |
| Rok vydání: |
2021 |
| Předmět: |
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| Zdroj: |
iScience, Vol 24, Iss 1, Pp 101952- (2021) |
| Druh dokumentu: |
article |
| ISSN: |
2589-0042 |
| DOI: |
10.1016/j.isci.2020.101952 |
| Popis: |
Summary: As a promising target for alternative antimicrobials, bacterial recombinase A (RecA) protein has attracted much attention for its roles in antibiotic-driven SOS response and mutagenesis. Naphthalene polysulfonated compounds (NPS) such as suramin have previously been explored as antibiotic adjuvants targeting RecA, although the underlying structural bases for RecA-ligand interactions remain obscure. Based on our in silico predictions and documented activity of NPS in vitro, we conclude that the analyzed NPS likely interact with Tyr103 (Y103) and other key residues in the ATPase activity center (pocket A). For validation, we generated recombinant RecA proteins (wild-type versus Y103 mutant) to determine the binding affinities for RecA protein interactions with suramin and underexamined NPS in isothermal titration calorimetry. The corresponding dissociation constants (Kd) ranged from 11.5 to 18.8 μM, and Y103 was experimentally shown to be critical to RecA-NPS interactions. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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