| Literature DB >> 33430384 |
Toru Yoshida1, Hideaki Tsuge2,3,4.
Abstract
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.Entities:
Keywords: ADP-ribosyltransferase; complex structure of enzyme and substrate; substrate recognition; target residue specificity
Mesh:
Substances:
Year: 2021 PMID: 33430384 PMCID: PMC7827354 DOI: 10.3390/toxins13010040
Source DB: PubMed Journal: Toxins (Basel) ISSN: 2072-6651 Impact factor: 4.546