ArticleThe Journal of biological chemistry2011
Structure of a ternary Naa50p (NAT5/SAN) N-terminal acetyltransferase complex reveals the molecular basis for substrate-specific acetylation.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.
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62 citing papers in PubMed, 96 citations in OpenAlex.
- NAA40 and NAC cooperate in co-translational histone acetylation in humans.Nature communications · 2026Article
- CUL4A-DDB1-DCAF10 is an N-recognin for N-terminally acetylated Src kinases.Nature communications · 2026Article
- 5-Thiohistidine N-Acetyltransferase from Proteiniphilum Saccharofermentans.Chembiochem : a European journal of chemical biology · 2025Article
- Structural basis of the catalytic and allosteric mechanism of bacterial acetyltransferase PatZ.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structure and mechanism of lysosome transmembrane acetylation by HGSNAT.Nature structural & molecular biology · 2024Article
- Impact of Protein NLife (Basel, Switzerland) · 2023Review
- Loss of Chloroplast GNAT Acetyltransferases Results in Distinct Metabolic Phenotypes in Arabidopsis.Plant & cell physiology · 2023Article
- Optimized bisubstrate inhibitors for the actin N-terminal acetyltransferase NAA80.Frontiers in chemistry · 2023Article
- From Nucleus to Membrane: A Subcellular Map of the N-Acetylation Machinery in Plants.International journal of molecular sciences · 2022Review
- Extended N-Terminal Acetyltransferase Naa50 in Filamentous Fungi Adds to Naa50 Diversity.International journal of molecular sciences · 2022Article
- Identification and characterization of a novel GNAT superfamily NMicrobial biotechnology · 2022Article
- Characterisation and preliminary functional analysis of N-acetyltransferase 13 from Schistosoma japonicum.BMC veterinary research · 2021Article
- Molecular mechanism of N-terminal acetylation by the ternary NatC complex.Structure (London, England : 1993) · 2021Article
- Structural basis of Naa20 activity towards a canonical NatB substrate.Communications biology · 2021Article
- Protein N-Terminal Acetylation: Structural Basis, Mechanism, Versatility, and Regulation.Trends in biochemical sciences · 2021Review
- Classification and phylogeny for the annotation of novel eukaryotic GNAT acetyltransferases.PLoS computational biology · 2020Article
- Divergent architecture of the heterotrimeric NatC complex explains N-terminal acetylation of cognate substrates.Nature communications · 2020Article
- NAA10 as a New Prognostic Marker for Cancer Progression.International journal of molecular sciences · 2020Review
- Article
- Loss of the Acetyltransferase NAA50 Induces Endoplasmic Reticulum Stress and Immune Responses and Suppresses Growth.Plant physiology · 2020Article
2 more citing papers are in PubMed but not listed here.
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3 authors at 2 institutions in 2 countries.
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Abstract
The co-translational modification of N-terminal acetylation is ubiquitous among eukaryotes and has been reported to have a wide range of biological effects. The human N-terminal acetyltransferase (NAT) Naa50p (NAT5/SAN) acetylates the α-amino group of proteins containing an N-terminal methionine residue and is essential for proper sister chromatid cohesion and chromosome condensation. The elevated activity of NATs has also been correlated with cancer, making these enzymes attractive therapeutic targets. We report the x-ray crystal structure of Naa50p bound to a native substrate peptide fragment and CoA. We found that the peptide backbone of the substrate is anchored to the protein through a series of backbone hydrogen bonds with the first methionine residue specified through multiple van der Waals contacts, together creating an α-amino methionine-specific pocket. We also employed structure-based mutagenesis; the results support the importance of the α-amino methionine-specific pocket of Naa50p and are consistent with the proposal that conserved histidine and tyrosine residues play important catalytic roles. Superposition of the ternary Naa50p complex with the peptide-bound Gcn5 histone acetyltransferase revealed that the two enzymes share a Gcn5-related N-acetyltransferase fold but differ in their respective substrate-binding grooves such that Naa50p can accommodate only an α-amino substrate and not a side chain lysine substrate that is acetylated by lysine acetyltransferase enzymes such as Gcn5. The structure of the ternary Naa50p complex also provides the first molecular scaffold for the design of NAT-specific small molecule inhibitors with possible therapeutic applications.
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