3F3M

Six Crystal Structures of Two Phosphopantetheine Adenylyltransferases Reveal an Alternative Ligand Binding Mode and an Associated Structural Change

3F3M の概要

• エントリーDOI: 10.2210/pdb3f3m/pdb
• 関連するPDBエントリー: 3F3I 3F3J 3F3L 3F3N 3F3O
• 分子名称: Phosphopantetheine adenylyltransferase, 3'-PHOSPHATE-ADENOSINE-5'-PHOSPHATE SULFATE (3 entities in total)
• 機能のキーワード: phosphopantetheine adenylyltransferase, ppat, coenzyme a biosynthetic pathway, coenzyme a biosynthesis, nucleotidyltransferase, transferase
• 由来する生物種: Staphylococcus aureus
• 細胞内の位置: Cytoplasm (By similarity): P63820
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19975.57

構造登録者

Lee, H.H.,Yoon, H.J.,Suh, S.W. (登録日: 2008-10-31, 公開日: 2009-10-20, 最終更新日: 2023-11-01)

主引用文献

Lee, H.H.,Yoon, H.J.,Kang, J.Y.,Park, J.H.,Kim, D.J.,Choi, K.H.,Lee, S.K.,Song, J.,Kim, H.J.,Suh, S.W.
The structure of Staphylococcus aureus phosphopantetheine adenylyltransferase in complex with 3'-phosphoadenosine 5'-phosphosulfate reveals a new ligand-binding mode
Acta Crystallogr.,Sect.F, 65:987-991, 2009

PubMed Abstract: 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.

PubMed: 19851003
DOI: 10.1107/S1744309109036616

実験手法

X-RAY DIFFRACTION (2.4 Å)