ArticleProtein science : a publication of the Protein Society2016
Structure of the sirtuin-linked macrodomain SAV0325 from Staphylococcus aureus.
Article in Protein science : a publication of the Protein Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 14 citations in OpenAlex.
- Staphylococcus aureus exploits lipoic acid salvage to combat host oxidative stress.Cell reports · 2025Article
- Family-wide analysis of human macrodomains reveals novel activities and identifies PARG as most efficient ADPr-RNA hydrolase.Communications biology · 2025Article
- Beyond protein modification: the rise of non-canonical ADP-ribosylation.The Biochemical journal · 2022Article
- Molecular Tools for the Study of ADP-Ribosylation: A Unified and Versatile Method to Synthesise Native Mono-ADP-Ribosylated Peptides.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- ADP-ribosylation systems in bacteria and viruses.Computational and structural biotechnology journal · 2021Review
- Bacterial Sirtuins Overview: An Open Niche to Explore.Frontiers in microbiology · 2021Review
- (ADP-ribosyl)hydrolases: structure, function, and biology.Genes & development · 2020Review
- A computational knowledge-base elucidates the response of Staphylococcus aureus to different media types.PLoS computational biology · 2019Article
- The macro domain as fusion tag for carrier-driven crystallization.Protein science : a publication of the Protein Society · 2017Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Cells use the post-translational modification ADP-ribosylation to control a host of biological activities. In some pathogenic bacteria, an operon-encoded mono-ADP-ribosylation cycle mediates response to host-induced oxidative stress. In this system, reversible mono ADP-ribosylation of a lipoylated target protein represses oxidative stress response. An NAD(+) -dependent sirtuin catalyzes the single ADP-ribose (ADPr) addition, while a linked macrodomain-containing protein removes the ADPr. Here we report the crystal structure of the sitruin-linked macrodomain protein from Staphylococcus aureus, SauMacro (also known as SAV0325) to 1.75-Å resolution. The monomeric SauMacro bears a previously unidentified Zn(2+) -binding site that putatively aids in substrate recognition and catalysis. An amino-terminal three-helix bundle motif unique to this class of macrodomain proteins provides a structural scaffold for the Zn(2+) site. Structural features of the enzyme further indicate a cleft proximal to the Zn(2+) binding site appears well suited for ADPr binding, while a deep hydrophobic channel in the protein core is suitable for binding the lipoate of the lipoylated protein target.
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