7L1K

Cryo-EM structure of S. Pombe NatC complex with a Bisubstrate inhibitor and inositol hexaphosphate

Summary for 7L1K

• Entry DOI: 10.2210/pdb7l1k/pdb
• EMDB information: 23110
• Descriptor: N-alpha-acetyltransferase 30, N-alpha-acetyltransferase 35, NatC auxiliary subunit, N-alpha-acetyltransferase 38, NatC auxiliary subunit, ... (6 entities in total)
• Functional Keywords: natb, naa20, naa25, transferase
• Biological source: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast); More
• Total number of polymer chains: 4
• Total formula weight: 113423.36

Authors

Deng, S.,Marmorstein, R. (deposition date: 2020-12-14, release date: 2021-05-12, Last modification date: 2024-05-29)

Primary citation

Deng, S.,Gottlieb, L.,Pan, B.,Supplee, J.,Wei, X.,Petersson, E.J.,Marmorstein, R.
Molecular mechanism of N-terminal acetylation by the ternary NatC complex.
Structure, 29:1094-, 2021

PubMed Abstract: 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), 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 binds tightly to NatC to stabilize the complex. We also describe the molecular basis for IP-mediated NatC complex stabilization and the overlapping yet distinct substrate profiles of NatC and NatE.

PubMed: 34019809
DOI: 10.1016/j.str.2021.05.003

Experimental method

ELECTRON MICROSCOPY (3.16 Å)