Author: Appel, C. Denise; Feld, Geoffrey K.; Wallace, Bret D.; Williams, R. Scott
Title: Structure of the sirtuinâ€linked macrodomain SAV0325 from Staphylococcus aureus Cord-id: tzxnlw0j Document date: 2016_7_7
ID: tzxnlw0j
Snippet: Cells use the postâ€translational modification ADPâ€ribosylation to control a host of biological activities. In some pathogenic bacteria, an operonâ€encoded monoâ€ADPâ€ribosylation cycle mediates response to hostâ€induced oxidative stress. In this system, reversible mono ADPâ€ribosylation of a lipoylated target protein represses oxidative stress response. An NAD(+)â€dependent sirtuin catalyzes the single ADPâ€ribose (ADPr) addition, while a linked macrodomainâ€containing protein remove
Document: Cells use the postâ€translational modification ADPâ€ribosylation to control a host of biological activities. In some pathogenic bacteria, an operonâ€encoded monoâ€ADPâ€ribosylation cycle mediates response to hostâ€induced oxidative stress. In this system, reversible mono ADPâ€ribosylation of a lipoylated target protein represses oxidative stress response. An NAD(+)â€dependent sirtuin catalyzes the single ADPâ€ribose (ADPr) addition, while a linked macrodomainâ€containing protein removes the ADPr. Here we report the crystal structure of the sitruinâ€linked macrodomain protein from Staphylococcus aureus, SauMacro (also known as SAV0325) to 1.75â€Ã… resolution. The monomeric SauMacro bears a previously unidentified Zn(2+)â€binding site that putatively aids in substrate recognition and catalysis. An aminoâ€terminal threeâ€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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