7YQ1

Crystal structure of adenosine 5'-phosphosulfate kinase from Archaeoglobus fulgidus in complex with AMP-PNP and APS

7YQ1 の概要

• エントリーDOI: 10.2210/pdb7yq1/pdb
• 分子名称: Adenylyl-sulfate kinase, ADENOSINE-5'-PHOSPHOSULFATE, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (7 entities in total)
• 機能のキーワード: aps kinase, archaea, transferase
• 由来する生物種: Archaeoglobus fulgidus
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 127045.35

構造登録者

Kawakami, T.,Teramoto, T.,Kakuta, Y. (登録日: 2022-08-05, 公開日: 2023-01-18, 最終更新日: 2023-11-29)

主引用文献

Kawakami, T.,Teramoto, T.,Kakuta, Y.
Crystal structure of adenosine 5'-phosphosulfate kinase isolated from Archaeoglobus fulgidus.
Biochem.Biophys.Res.Commun., 643:105-110, 2022

PubMed Abstract: The 3'-phosphoadenosine-5'-phosphosulfate (PAPS) molecule is essential during enzyme-catalyzed sulfation reactions as a sulfate donor and is an intermediate in the reduction of sulfate to sulfite in the sulfur assimilation pathway. PAPS is produced through a two-step reaction involving ATP sulfurylase and adenosine 5'-phosphosulfate (APS) kinase enzymes/domains. However, archaeal APS kinases have not yet been characterized and their mechanism of action remains unclear. Here, we first structurally characterized APS kinase from the hyperthermophilic archaeon Archaeoglobus fulgidus, (AfAPSK). We demonstrated the PAPS production activity of AfAPSK at the optimal growth temperature (83 °C). Furthermore, we determined the two crystal structures of AfAPSK: ADP complex and ATP analog adenylyl-imidodiphosphate (AMP-PNP)/Mg/APS complex. Structural and complementary mutational analyses revealed the catalytic and substrate recognition mechanisms of AfAPSK. This study also hints at the molecular basis behind the thermal stability of AfAPSK.

PubMed: 36592583
DOI: 10.1016/j.bbrc.2022.12.081

実験手法

X-RAY DIFFRACTION (1.91 Å)