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TitleRedefining the role of the EryM acetyltransferase in natural product biosynthetic pathways.
Journal, issue, pagesStructure, Vol. 33, Page 1352-1361.e3, Year 2025
Publish dateMar 6, 2025 (structure data deposition date)
AuthorsLi, Y. / Liu, X. / Harris, N.R. / Roberts, J.R. / Valdivia, E.M. / Ji, X. / Smith, J.L.
External linksStructure / PubMed:40516533
MethodsX-ray diffraction
Resolution2.5 - 3 Å
Structure data

PDB-9nnq:
GNAT family acetyltransferase EryM
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-9nnr:
GNAT family acetyltransferase EryM in complex with Acetyl-CoA
Method: X-RAY DIFFRACTION / Resolution: 2.9 Å

PDB-9nns:
Flavin-dependent N5-ornithine monooxygenase EtcB
Method: X-RAY DIFFRACTION / Resolution: 3 Å

PDB-9oa7:
GNAT family acetyltransferase EryM SeMet
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-SO4:
SULFATE ION

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-ACO:
ACETYL COENZYME *A

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

Source
  • saccharopolyspora erythraea (bacteria)
KeywordsTRANSFERASE / GNAT / acetyltransferase / erythrochelin / FLAVOPROTEIN / FAD-dependent / monooxygenase

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