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• W3025657245 abstract "Abstract 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 Parkinson’s disease pathogenesis 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 Candida albicans 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." @default.
• W3025657245 created "2020-05-21" @default.
• W3025657245 creator A5032949179 @default.
• W3025657245 creator A5061620397 @default.
• W3025657245 creator A5078577448 @default.
• W3025657245 creator A5091398901 @default.
• W3025657245 creator A5054632049 @default.
• W3025657245 date "2020-05-13" @default.
• W3025657245 modified "2023-10-14" @default.
• W3025657245 title "Molecular Basis for N-terminal Alpha-Synuclein Acetylation by Human NatB" @default.
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• W3025657245 doi "https://doi.org/10.1101/2020.05.11.089318" @default.
• W3025657245 hasPublicationYear "2020" @default.
• W3025657245 type Work @default.
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• W3025657245 hasAuthorship W3025657245A5078577448 @default.
• W3025657245 hasAuthorship W3025657245A5091398901 @default.

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