Fig. 4: METAP1 and NAA40 form a multienzyme assembly on the ribosome in vitro.
From: NAA40 and NAC cooperate in co-translational histone acetylation in humans
Local resolution filtered cryo-EM maps (top) and molecular models (bottom) of a METAP1-State1 and b State2. c Overview of the NAA40-METAP1-NAC ribosome binding site for State1 (top, METAP1-S1) and State2 (bottom, METAP1-S2). Molecular models of NAA40, METAP1 and NAC as assembled around the peptide exit for d State1 and e State2. Molecular models for METAP1 were substituted with AF3 predictions for the METAP1 zinc finger—NACB C-terminus interaction that is not visible in our structure. Flexible connection between the NACB C-terminus and the NACA-UBA domain with the NAC globular domain is indicated. f Overlay of METAP1 State1 and State2 indicating the distances between the METAP1 active sites and the peptide exit site. Molecular models are shown as surface representations, and the NAC globular domain was omitted for clarity. g Cartoon representation illustrating the simultaneous recruitment of NAA40 and METAP1 via NAC.
