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TitleMolecular basis for N-terminal alpha-synuclein acetylation by human NatB.
Journal, issue, pagesElife, Vol. 9, Year 2020
Publish dateSep 4, 2020
AuthorsSunbin Deng / Buyan Pan / Leah Gottlieb / E James Petersson / Ronen Marmorstein /
PubMed AbstractNatB is one of three major N-terminal acetyltransferase (NAT) complexes (NatA-NatC), which co-translationally acetylate the N-termini of eukaryotic proteins. Its substrates account for about 21% of ...NatB is one of three major N-terminal acetyltransferase (NAT) complexes (NatA-NatC), which co-translationally acetylate the N-termini of eukaryotic proteins. Its substrates account for about 21% of the human proteome, including well known proteins such as actin, tropomyosin, CDK2, and α-synuclein (αSyn). Human NatB (hNatB) mediated N-terminal acetylation of αSyn has been demonstrated to play key roles in the pathogenesis of Parkinson's disease and as a potential therapeutic target for hepatocellular carcinoma. Here we report the cryo-EM structure of hNatB bound to a CoA-αSyn conjugate, together with structure-guided analysis of mutational effects on catalysis. This analysis reveals functionally important differences with human NatA and NatB, resolves key hNatB protein determinants for αSyn N-terminal acetylation, and identifies important residues for substrate-specific recognition and acetylation by NatB enzymes. These studies have implications for developing small molecule NatB probes and for understanding the mode of substrate selection by NAT enzymes.
External linksElife / PubMed:32885784 / PubMed Central
MethodsEM (single particle)
Resolution3.46 Å
Structure data

21307

6vp9

EMDB-21307, PDB-6vp9:
Cryo-EM structure of human NatB complex
Method: EM (single particle) / Resolution: 3.46 Å

Chemicals

ChemComp-CMC:
CARBOXYMETHYL COENZYME *A

Source
  • homo sapiens (human)
  • Escherichia coli (E. coli)
  • escherichia coli k-12 (bacteria)
KeywordsTRANSFERASE / NatB / NAA20 / NAA25

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