4.7 Review

Common Mechanism for Target Specificity of Protein- and DNA-Targeting ADP-Ribosyltransferases

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

  1. Strategic Research Foundation
  2. MEXT KAKENHI Grant [23121529, 25121733]
  3. JSPS KAKENHI [15K08289, 17K15095]
  4. Kyoto Sangyo University [H1901]
  5. Grants-in-Aid for Scientific Research [23121529, 17K15095, 15K08289] Funding Source: KAKEN

向作者/读者索取更多资源

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.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.7
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据