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TitleStructural insights into interdomain interactions in APS kinase.
Journal, issue, pagesJ Struct Biol X, Vol. 13, Page 100147, Year 2026
Publish dateMay 15, 2026
AuthorsRyo Hatanaka / Yukiko Ohsumi / Hiroki Matsui / Ayuna Inoguchi / Hina Yuasa / Fumika Mi-Ichi / Jun-Ichi Kishikawa / Tomoo Shiba /
PubMed AbstractThe biosynthetic pathway of 3'-phosphoadenosine-5'-phosphosulfate (PAPS) is a universal and essential metabolic process in many organisms, providing the activated sulfate donor required for the ...The biosynthetic pathway of 3'-phosphoadenosine-5'-phosphosulfate (PAPS) is a universal and essential metabolic process in many organisms, providing the activated sulfate donor required for the synthesis of diverse sulfated metabolites. However, this pathway has undergone substantial evolutionary diversification among species. In , PAPS biosynthesis occurs within the mitosomes, mitochondrion-related organelles (MROs), representing a distinctive example of lineage-specific evolutionary adaptation. PAPS synthesis proceeds through a conserved two-step process, which is sequentially catalyzed by ATP sulfurylase (AS) and adenosine 5'-phosphosulfate (APS) kinase (APSK). In this study, we focused on APSK (APSK). APSK contains an additional AS-like domain (SLD), although its functional role remains unclear. Here, we determined the crystal structure of full-length APSK at 2.60 Å resolution and the structure of the truncated APSK lacking APS kinase domain (KD) (APSK) at 2.10 Å resolution. Structural analyses revealed that the SLD engages in dynamic contacts with the KD. Furthermore, deletion of the domain and mutational analyses indicated that the SLD significantly influences the catalytic activity of the KD. Based on these findings, we propose a new regulatory mechanism in which transient interdomain interactions modulate APS kinase activity, representing an unique evolutionary adaptation of .
External linksJ Struct Biol X / PubMed:42212241 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.1 - 3.44 Å
Structure data

EMDB-80056: APS kinase from Entamoeba histolytica
Method: EM (single particle) / Resolution: 3.44 Å

PDB-23vk:
Crystal structure of full-length of APS kinase from Entamoeba histolytica
Method: X-RAY DIFFRACTION / Resolution: 2.595 Å

PDB-23vl:
Crystal structure of AS-like domain of APS kinase from Entamoeba histolytica
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • entamoeba histolytica (eukaryote)
KeywordsTRANSFERASE / KINASE / sulfate activation / SULFURYLASE-LIKE DOMAIN / SULFURYLASE-lLIKE

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