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Common Mechanism for Target Specificity of Protein- and DNA-Targeting ADP-Ribosyltransferases
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 speci...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7827354/ https://www.ncbi.nlm.nih.gov/pubmed/33430384 http://dx.doi.org/10.3390/toxins13010040 |
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author | Yoshida, Toru Tsuge, Hideaki |
author_facet | Yoshida, Toru Tsuge, Hideaki |
author_sort | Yoshida, Toru |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-7827354 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-78273542021-01-25 Common Mechanism for Target Specificity of Protein- and DNA-Targeting ADP-Ribosyltransferases Yoshida, Toru Tsuge, Hideaki Toxins (Basel) Review 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. MDPI 2021-01-07 /pmc/articles/PMC7827354/ /pubmed/33430384 http://dx.doi.org/10.3390/toxins13010040 Text en © 2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Yoshida, Toru Tsuge, Hideaki Common Mechanism for Target Specificity of Protein- and DNA-Targeting ADP-Ribosyltransferases |
title | Common Mechanism for Target Specificity of Protein- and DNA-Targeting ADP-Ribosyltransferases |
title_full | Common Mechanism for Target Specificity of Protein- and DNA-Targeting ADP-Ribosyltransferases |
title_fullStr | Common Mechanism for Target Specificity of Protein- and DNA-Targeting ADP-Ribosyltransferases |
title_full_unstemmed | Common Mechanism for Target Specificity of Protein- and DNA-Targeting ADP-Ribosyltransferases |
title_short | Common Mechanism for Target Specificity of Protein- and DNA-Targeting ADP-Ribosyltransferases |
title_sort | common mechanism for target specificity of protein- and dna-targeting adp-ribosyltransferases |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7827354/ https://www.ncbi.nlm.nih.gov/pubmed/33430384 http://dx.doi.org/10.3390/toxins13010040 |
work_keys_str_mv | AT yoshidatoru commonmechanismfortargetspecificityofproteinanddnatargetingadpribosyltransferases AT tsugehideaki commonmechanismfortargetspecificityofproteinanddnatargetingadpribosyltransferases |