Open AccessThe structure of Staphylococcus aureus phosphopantetheine adenylyltransferase in complex with 3′‐phosphoadenosine 5′‐phosphosulfate reveals a new ligand‐binding mode
Author(s) -
Lee Hyung Ho,
Yoon HyeJin,
Kang Ji Yong,
Park Ji Hyeon,
Kim Do Jin,
Choi KwangHyun,
Lee SeungKyu,
Song Jinsu,
Kim HieJoon,
Suh Se Won
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109036616
Subject(s) - ligand (biochemistry) , stereochemistry , coenzyme a , cofactor , chemistry , transferase , binding site , biochemistry , biology , enzyme , receptor , reductase
Bacterial phosphopantetheine adenylyltransferase (PPAT) catalyzes the penultimate step in the coenzyme A (CoA) biosynthetic pathway. It catalyzes the reversible transfer of an adenylyl group from ATP to 4′‐phosphopantetheine (Ppant) to form dephospho‐CoA (dPCoA) and pyrophosphate. Previous structural studies have revealed how several ligands are recognized by bacterial PPATs. ATP, ADP, Ppant and dPCoA bind to the same binding site in a highly similar manner, while CoA binds to a partially overlapping site in a different mode. To provide further structural insights into ligand binding, the crystal structure of Staphylococcus aureus PPAT was solved in a binary complex with 3′‐phosphoadenosine 5′‐phosphosulfate (PAPS). This study unexpectedly revealed a new mode of ligand binding to PPAT, thus providing potentially useful information for structure‐based discovery of inhibitors of bacterial PPATs.