Structural highlights
Function
NAA38_SCHPO
Publication Abstract from PubMed
Protein N-terminal acetylation is predominantly a ribosome-associated modification, with NatA-E serving as the major enzymes. NatC is the most unusual of these enzymes, containing one Naa30 catalytic subunit and two auxiliary subunits, Naa35 and Naa38; and substrate selectivity profile that overlaps with NatE. Here, we report the cryoelectron microscopy structure of S. pombe NatC with a NatE/C-type bisubstrate analog and inositol hexaphosphate (IP(6)), and associated biochemistry studies. We find that the presence of three subunits is a prerequisite for normal NatC acetylation activity in yeast and that IP(6) binds tightly to NatC to stabilize the complex. We also describe the molecular basis for IP(6)-mediated NatC complex stabilization and the overlapping yet distinct substrate profiles of NatC and NatE.
Molecular mechanism of N-terminal acetylation by the ternary NatC complex.,Deng S, Gottlieb L, Pan B, Supplee J, Wei X, Petersson EJ, Marmorstein R Structure. 2021 Oct 7;29(10):1094-1104.e4. doi: 10.1016/j.str.2021.05.003. Epub , 2021 May 20. PMID:34019809[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Deng S, Gottlieb L, Pan B, Supplee J, Wei X, Petersson EJ, Marmorstein R. Molecular mechanism of N-terminal acetylation by the ternary NatC complex. Structure. 2021 Oct 7;29(10):1094-1104.e4. PMID:34019809 doi:10.1016/j.str.2021.05.003
