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Structure paper

TitleStructural basis of HypK regulating N-terminal acetylation by the NatA complex.
Journal, issue, pagesNat Commun, Vol. 8, Page 15726-15726, Year 2017
Publish dateApr 10, 2017 (structure data deposition date)
AuthorsWeyer, F.A. / Gumiero, A. / Lapouge, K. / Bange, G. / Kopp, J. / Sinning, I.
External linksNat Commun / PubMed:28585574
MethodsX-ray diffraction
Resolution2.602 - 3.1 Å
Structure data

PDB-5nnp:
Structure of Naa15/Naa10 bound to HypK-THB
Method: X-RAY DIFFRACTION / Resolution: 2.602 Å

PDB-5nnr:
Structure of Naa15/Naa10 bound to HypK-THB
Method: X-RAY DIFFRACTION / Resolution: 3.1 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-PO4:
PHOSPHATE ION

ChemComp-CMC:
CARBOXYMETHYL COENZYME *A

ChemComp-HOH:
WATER

Source
  • chaetomium thermophilum (strain dsm 1495 / cbs 144.50 / imi 039719) (fungus)
  • chaetomium thermophilum (fungus)
  • synthetic construct (others)
KeywordsTRANSFERASE / N-acetylation / NATs / Naa15 / Naa10 / HypK / NatA / Nat1 / Ard1 / bisubstrate analogue

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