Journal
STRUCTURE
Volume 24, Issue 7, Pages 1044-1056Publisher
CELL PRESS
DOI: 10.1016/j.str.2016.04.020
Keywords
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Funding
- Norwegian Cancer Society
- Bergen Research Foundation BFS
- Research Council of Norway [230865]
- Western Norway Regional Health Authority
- NIH [R01 GM060293, T32 GM071339]
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N-Terminal acetylation is a common and important protein modification catalyzed by N-terminal acetyl-transferases (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 sub-strate-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.
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