9t6c | pdb_00009t6c

NAA40-NAC bound active human 80S

spinqualitylabelsall models 9t6c, resolution 2.91Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9t6c is a 10 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.91Å Ligands: MG, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RL8_HUMAN Publication Abstract from PubMed N-terminal acetylation is an abundant and predominantly co-translational modification in eukaryotes that profoundly affects folding, compartmentalization fidelity and turnover of target proteins. Unlike other N-acetyltransferases, human NatD is composed solely of the catalytic subunit NAA40 and exclusively modifies histone proteins H2A and H4. However, the molecular details of co-translational NAA40 activity have remained elusive. Here, we show biochemically and by cryo-EM how NAA40 activity is coordinated at the ribosomal peptide tunnel exit involving the NAC complex. We demonstrate that the NAA40-NAC interaction is required for efficient ribosome binding and histone acetylation. Furthermore, we provide insights on the potential coordination of methionine removal and subsequent NAA40-mediated acetylation by formation of a multienzyme complex on the ribosome involving METAP1. Therefore, our results illustrate the details of N-terminal histone acetylation by NAA40 and highlight the role of NAC as a general coordinator of nascent protein modification. NAA40 and NAC cooperate in co-translational histone acetylation in humans.,Guan D, Denk T, Klavaris A, Thoms M, Berninghausen O, Beatrix B, Kirmizis A, Beckmann R Nat Commun. 2026 Mar 12;17(1):2486. doi: 10.1038/s41467-026-70279-5. PMID:41820326 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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