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TitleMolecular mechanism of N-terminal acetylation by the ternary NatC complex.
Journal, issue, pagesStructure, Vol. 29, Issue 10, Page 1094-11104.e4, Year 2021
Publish dateOct 7, 2021
AuthorsSunbin Deng / Leah Gottlieb / Buyan Pan / Julianna Supplee / Xuepeng Wei / E James Petersson / Ronen Marmorstein /
PubMed AbstractProtein N-terminal acetylation is predominantly a ribosome-associated modification, with NatA-E serving as the major enzymes. NatC is the most unusual of these enzymes, containing one Naa30 catalytic ...Protein N-terminal acetylation is predominantly a ribosome-associated modification, with NatA-E serving as the major enzymes. NatC is the most unusual of these enzymes, containing one Naa30 catalytic subunit and two auxiliary subunits, Naa35 and Naa38; and substrate selectivity profile that overlaps with NatE. Here, we report the cryoelectron microscopy structure of S. pombe NatC with a NatE/C-type bisubstrate analog and inositol hexaphosphate (IP), and associated biochemistry studies. We find that the presence of three subunits is a prerequisite for normal NatC acetylation activity in yeast and that IP binds tightly to NatC to stabilize the complex. We also describe the molecular basis for IP-mediated NatC complex stabilization and the overlapping yet distinct substrate profiles of NatC and NatE.
External linksStructure / PubMed:34019809 / PubMed Central
MethodsEM (single particle)
Resolution3.16 Å
Structure data

23110

7l1k

EMDB-23110, PDB-7l1k:
Cryo-EM structure of S. Pombe NatC complex with a Bisubstrate inhibitor and inositol hexaphosphate
Method: EM (single particle) / Resolution: 3.16 Å

Chemicals

ChemComp-IHP:
INOSITOL HEXAKISPHOSPHATE

ChemComp-CMC:
CARBOXYMETHYL COENZYME *A

Source
  • Schizosaccharomyces pombe (fission yeast)
  • schizosaccharomyces pombe (strain 972 / atcc 24843) (yeast)
  • homo sapiens (human)
KeywordsTRANSFERASE / NatB / NAA20 / NAA25

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