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

Toxins

Hideaki Tsuge¹  Toru Yoshida² 

[1] Faculty of Life Sciences, Kyoto Sangyo University, Kamigamo-motoyama, Kita-ku, Kyoto 603-8555, Japan;Faculty of Science, Japan Women’s University, 2-8-1 Mejirodai, Bunkyo-ku, Tokyo 112-8681, Japan;

关键词: ADP-ribosyltransferase;    substrate recognition;    target residue specificity;    complex structure of enzyme and substrate;   

DOI  :  10.3390/toxins13010040

来源: DOAJ

【 摘 要 】

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.

【 授权许可】

Unknown