5KIV

Crystal structure of SauMacro (SAV0325)

Summary for 5KIV

• Entry DOI: 10.2210/pdb5kiv/pdb
• Descriptor: Protein-ADP-ribose hydrolase, ZINC ION, 1,2-ETHANEDIOL, ... (5 entities in total)
• Functional Keywords: macrodomain, zn binding, lipoate binding, adp-ribose, hydrolase
• Biological source: Staphylococcus aureus
• Total number of polymer chains: 1
• Total formula weight: 30986.83

Authors

Williams, R.S.,Appel, C.D.,Feld, G.K.,Wallace, B.D. (deposition date: 2016-06-17, release date: 2016-07-13, Last modification date: 2023-09-27)

Primary citation

Appel, C.D.,Feld, G.K.,Wallace, B.D.,Williams, R.S.
Structure of the sirtuin-linked macrodomain SAV0325 from Staphylococcus aureus.
Protein Sci., 25:1682-1691, 2016

PubMed 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.

PubMed: 27345688
DOI: 10.1002/pro.2974

Experimental method

X-RAY DIFFRACTION (1.75 Å)