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- W2425379846 abstract "N-Terminal acetylation is a common and important protein modification catalyzed by N-terminal acetyltransferases (NATs). Six human NATs (NatA-NatF) contain one catalytic subunit each, Naa10 to Naa60, respectively. In contrast to the ribosome-associated NatA to NatE, NatF/Naa60 specifically associates with Golgi membranes and acetylates transmembrane proteins. To gain insight into the molecular basis for the function of Naa60, we developed an Naa60 bisubstrate CoA-peptide conjugate inhibitor, determined its X-ray structure when bound to CoA and inhibitor, and carried out biochemical experiments. We show that Naa60 adapts an overall fold similar to that of the catalytic subunits of ribosome-associated NATs, but with the addition of two novel elongated loops that play important roles in substrate-specific binding. One of these loops mediates a dimer to monomer transition upon substrate-specific binding. Naa60 employs a catalytic mechanism most similar to Naa50. Collectively, these data reveal the molecular basis for Naa60-specific acetyltransferase activity with implications for its Golgi-specific functions." @default.
- W2425379846 created "2016-06-24" @default.
- W2425379846 creator A5027097671 @default.
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- W2425379846 date "2016-07-01" @default.
- W2425379846 modified "2023-10-12" @default.
- W2425379846 title "Crystal Structure of the Golgi-Associated Human Nα-Acetyltransferase 60 Reveals the Molecular Determinants for Substrate-Specific Acetylation" @default.
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- W2425379846 doi "https://doi.org/10.1016/j.str.2016.04.020" @default.
- W2425379846 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4938767" @default.
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