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Structure paper

TitleStructure-Activity Relationship of an All-alpha-helical Prenyltransferase Reveals the Mechanism of Indole Prenylation.
Journal, issue, pagesBiochemistry, Vol. 64, Page 4196-4205, Year 2025
Publish dateMay 23, 2025 (structure data deposition date)
AuthorsOshiro, T. / Uehara, S. / Suto, A. / Tanaka, Y. / Ito, T. / Kodera, Y. / Matsui, T.
External linksBiochemistry / PubMed:40968638
MethodsX-ray diffraction
Resolution2 - 2.8 Å
Structure data

PDB-9v4g:
Prenyltransferase Ord1 wild type
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-9v4h:
Prenyltransferase Ord1 Q216A-FSPP
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-9v4i:
Prenyltransferase Ord1 D219A
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-9v4j:
Prenyltransferase Ord1 Wild type-FSPP
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

ChemComp-FPS:
S-[(2E,6E)-3,7,11-TRIMETHYLDODECA-2,6,10-TRIENYL] TRIHYDROGEN THIODIPHOSPHATE

ChemComp-MG:
Unknown entry

Source
  • streptomyces sp. ks84 (bacteria)
KeywordsTRANSFERASE / Prenyltransferase

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