Molecular mechanism of N-terminal acetylation by the ternary NatC complex.
作者： E James Petersson , Ronen Marmorstein , Xuepeng Wei , Sunbin Deng , Buyan Pan
DOI: 10.1016/J.STR.2021.05.003
关键词:
摘要: Summary Protein N-terminal acetylation is predominantly a ribosome-associated modification, with NatA-E serving as the major enzymes. NatC most unusual of these enzymes, containing one Naa30 catalytic subunit and two auxiliary subunits, Naa35 Naa38; substrate selectivity profile that overlaps NatE. Here, we report cryoelectron microscopy structure S. pombe NatE/C-type bisubstrate analog inositol hexaphosphate (IP6), associated biochemistry studies. We find presence three subunits prerequisite for normal activity in yeast IP6 binds tightly to stabilize complex. also describe molecular basis IP6-mediated complex stabilization overlapping yet distinct profiles
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