期刊
TOXINS
卷 13, 期 1, 页码 -出版社
MDPI
DOI: 10.3390/toxins13010040
关键词
ADP-ribosyltransferase; substrate recognition; target residue specificity; complex structure of enzyme and substrate
资金
- Strategic Research Foundation
- MEXT KAKENHI Grant [23121529, 25121733]
- JSPS KAKENHI [15K08289, 17K15095]
- Kyoto Sangyo University [H1901]
- Grants-in-Aid for Scientific Research [23121529, 17K15095, 15K08289] Funding Source: KAKEN
Many bacterial pathogens utilize ADP-ribosyltransferases (ARTs) as virulence factors, with specific residue modifications on their substrates. Common mechanisms of target residue specificity exist among protein- and DNA-targeting ARTs.
Many bacterial pathogens utilize ADP-ribosyltransferases (ARTs) as virulence factors. The critical aspect of ARTs is their target specificity. Each individual ART modifies a specific residue of its substrates, which could be proteins, DNA, or antibiotics. However, the mechanism underlying this specificity is poorly understood. Here, we review the substrate recognition mechanism and target residue specificity based on the available complex structures of ARTs and their substrates. We show that there are common mechanisms of target residue specificity among protein- and DNA-targeting ARTs.
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