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TitleStructure and Mechanism of Acetylation by the N-Terminal Dual Enzyme NatA/Naa50 Complex.
Journal, issue, pagesStructure, Vol. 27, Page 1057-, Year 2019
Publish dateFeb 15, 2019 (structure data deposition date)
AuthorsDeng, S. / Magin, R.S. / Wei, X. / Pan, B. / Petersson, E.J. / Marmorstein, R.
External linksStructure / PubMed:31155310
MethodsX-ray diffraction
Resolution2.702 Å
Structure data

PDB-6o07:
Structure and mechanism of acetylation by the N-terminal dual enzyme NatA/Naa50 complex
Method: X-RAY DIFFRACTION / Resolution: 2.702 Å

Chemicals

ChemComp-CL:
Unknown entry

ChemComp-GOL:
GLYCEROL

ChemComp-ACO:
ACETYL COENZYME *A

ChemComp-MLI:
MALONATE ION

ChemComp-IHP:
INOSITOL HEXAKISPHOSPHATE

ChemComp-EPE:
4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID / pH buffer*YM

ChemComp-HOH:
WATER

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsTRANSFERASE / N-terminal acetylation / protein complex / NatA / Naa50 / NatE

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