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TitleSpeG polyamine acetyltransferase enzyme from Bacillus thuringiensis forms a dodecameric structure and exhibits high catalytic efficiency.
Journal, issue, pagesJ. Struct. Biol., Vol. 210, Page 107506-107506, Year 2020
Publish dateJan 5, 2020 (structure data deposition date)
AuthorsTsimbalyuk, S. / Shornikov, A. / Thi Bich Le, V. / Kuhn, M.L. / Forwood, J.K.
External linksJ. Struct. Biol. / PubMed:32283314
MethodsX-ray diffraction
Resolution2.5 - 2.67 Å
Structure data

PDB-6vfm:
Crystal structure of SpeG allosteric polyamine acetyltransferase from Bacillus thuringiensis
Method: X-RAY DIFFRACTION / Resolution: 2.67 Å

PDB-6vfn:
Crystal structure of SpeG allosteric polyamine acetyltransferase from Bacillus thuringiensis in complex with spermine
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

Chemicals

ChemComp-SPM:
SPERMINE

Source
  • bacillus thuringiensis subsp. finitimus (strain ybt-020) (bacteria)
  • bacillus thuringiensis (bacteria)
KeywordsTRANSFERASE / SpeG / Allosteric enzyme / GNAT / Acetyltransferase

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