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TitleMolecular role of NAA38 in thermostability and catalytic activity of the human NatC N-terminal acetyltransferase.
Journal, issue, pagesStructure, Vol. 31, Issue 2, Page 166-173.e4, Year 2023
Publish dateFeb 2, 2023
AuthorsSunbin Deng / Sarah M Gardner / Leah Gottlieb / Buyan Pan / E James Petersson / Ronen Marmorstein /
PubMed AbstractN-terminal acetylation occurs on over 80% of human proteins and is catalyzed by a family of N-terminal acetyltransferases (NATs). All NATs contain a small catalytic subunit, while some also contain a ...N-terminal acetylation occurs on over 80% of human proteins and is catalyzed by a family of N-terminal acetyltransferases (NATs). All NATs contain a small catalytic subunit, while some also contain a large auxiliary subunit that facilitates catalysis and ribosome targeting for co-translational acetylation. NatC is one of the major NATs containing an NAA30 catalytic subunit, but uniquely contains two auxiliary subunits, large NAA35 and small NAA38. Here, we report the cryo-EM structures of human NatC (hNatC) complexes with and without NAA38, together with biochemical studies, to reveal that NAA38 increases the thermostability and broadens the substrate-specificity profile of NatC by ordering an N-terminal segment of NAA35 and reorienting an NAA30 N-terminal peptide binding loop for optimal catalysis, respectively. We also note important differences in engagement with a stabilizing inositol hexaphosphate molecule between human and yeast NatC. These studies provide new insights for the function and evolution of the NatC complex.
External linksStructure / PubMed:36638802 / PubMed Central
MethodsEM (single particle)
Resolution3.1 - 3.64 Å
Structure data

24070

7mx2

EMDB-24070, PDB-7mx2:
Cryo-EM structure of human ternary NatC complex with a Bisubstrate inhibitor
Method: EM (single particle) / Resolution: 3.64 Å

24393

7rb3

EMDB-24393, PDB-7rb3:
Cryo-EM structure of human binary NatC complex with a Bisubstrate inhibitor
Method: EM (single particle) / Resolution: 3.1 Å

Chemicals

ChemComp-CMC:
CARBOXYMETHYL COENZYME *A

ChemComp-MET:
METHIONINE / Methionine

ChemComp-LEU:
LEUCINE / Leucine

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / NatC / NAA30 / NAA35 / NAA38

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