Fig. 2: Molecular details of the NAA40-NAC ribosome interaction.
From: NAA40 and NAC cooperate in co-translational histone acetylation in humans
a Overview of the NAA40-NAC binding site at the peptide exit site. b Close ups of the interaction sites of the GNAT domain (left) and the N-terminal α0 helix (right) of NAA40 with the ribosome. c Details of the interactions of the positively charged residues of the NAA40 α0 helix and the unstructured N-terminus with rRNA helices H19, H24 and H46. d–g Close ups of the interactions of NAC with NAA40 and the ribosome. d NACB anchor-eL22 interaction. e Contacts of NAC beta-sandwich and NAA40 GNAT domain. f Comparison of the NAC globular domain positioning between active (green) and hibernating 80S (cyan). g NAA40-NACA-UBA domain.
