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Structure paper

TitleDivergent architecture of the heterotrimeric NatC complex explains N-terminal acetylation of cognate substrates.
Journal, issue, pagesNat Commun, Vol. 11, Page 5506-5506, Year 2020
Publish dateMar 27, 2020 (structure data deposition date)
AuthorsGrunwald, S. / Hopf, L.V.M. / Bock-Bierbaum, T. / Lally, C.C.M. / Spahn, C.M.T. / Daumke, O.
External linksNat Commun / PubMed:33139728
MethodsX-ray diffraction
Resolution2.397 - 2.994 Å
Structure data

PDB-6yga:
Crystal structure of the apo NatC complex
Method: X-RAY DIFFRACTION / Resolution: 2.397 Å

PDB-6ygb:
Crystal structure of the NatC complex bound to CoA
Method: X-RAY DIFFRACTION / Resolution: 2.451 Å

PDB-6ygc:
Crystal structure of the NatC complex bound to Arl3 peptide and CoA
Method: X-RAY DIFFRACTION / Resolution: 2.994 Å

PDB-6ygd:
Crystal structure of the NatC complex bound to Gag peptide and CoA
Method: X-RAY DIFFRACTION / Resolution: 2.752 Å

Chemicals

ChemComp-IOD:
IODIDE ION

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-COA:
COENZYME A

ChemComp-GOL:
GLYCEROL

Source
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
  • saccharomyces cerevisiae (brewer's yeast)
  • saccharomyces cerevisiae virus l-a
KeywordsTRANSFERASE / N-terminal acetylation / NAT / GNAT / acetyltransferase / Naa30 / Naa35 / Naa38 / Mak3 / Mak10 / Mak31

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