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TitleStructural and functional insights into an archaeal dUTPase reveal a subdomain-mediated mechanism for substrate recognition and evolutionary adaptation.
Journal, issue, pagesInt. J. Biol. Macromol., Vol. 335, Page 149194-149194, Year 2026
Publish dateAug 1, 2025 (structure data deposition date)
AuthorsChen, S.C. / Chou, C.C. / Chen, W.M. / Sheu, S.Y. / Huang, L.W. / Huang, C.H. / Chang, S.C. / Kuo, C.H. / Hsu, C.H.
External linksInt. J. Biol. Macromol. / PubMed:41308777
MethodsX-ray diffraction
Resolution1.45 - 1.53 Å
Structure data

PDB-9w59:
The structure of dUTPase from Methanosarcina mazei
Method: X-RAY DIFFRACTION / Resolution: 1.45 Å

PDB-9w5a:
The structure of dUTPase in complex with dUTP from Methanosarcina mazei
Method: X-RAY DIFFRACTION / Resolution: 1.53 Å

Chemicals

ChemComp-PO4:
PHOSPHATE ION

ChemComp-HOH:
WATER

ChemComp-DUT:
DEOXYURIDINE-5'-TRIPHOSPHATE

Source
  • methanosarcina mazei (archaea)
KeywordsHYDROLASE / Archaea; dUTPase; trimeric enzyme; crystal structure; subdomain I; evolutionary divergence

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