6o07 | pdb_00006o07

Structure and mechanism of acetylation by the N-terminal dual enzyme NatA/Naa50 complex

spinqualitylabelsall models 6o07, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6o07 is a 3 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACO, CL, EPE, GOL, IHP, MLI Activity: N-terminal methionine N(alpha)-acetyltransferase NatE, with EC number 2.3.1.258 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [NAT5_YEAST] Non-essential component of the NatA N-terminal acetyltransferase, which catalyzes acetylation of proteins beginning with Met-Ser, Met-Gly and Met-Ala. N-acetylation plays a role in normal eukaryotic translation and processing, protect against proteolytic degradation and protein turnover. [ARD1_YEAST] Catalytic component of the NatA N-terminal acetyltransferase, which catalyzes acetylation of proteins beginning with Met-Ser, Met-Gly and Met-Ala. N-acetylation plays a role in normal eukaryotic translation and processing, protect against proteolytic degradation and protein turnover. Publication Abstract from PubMed NatA co-translationally acetylates the N termini of over 40% of eukaryotic proteins and can associate with another catalytic subunit, Naa50, to form a ternary NatA/Naa50 dual enzyme complex (also called NatE). The molecular basis of association between Naa50 and NatA and the mechanism for how their association affects their catalytic activities in yeast and human are poorly understood. Here, we determined the X-ray crystal structure of yeast NatA/Naa50 as a scaffold to understand coregulation of NatA/Naa50 activity in both yeast and human. We find that Naa50 makes evolutionarily conserved contacts to both the Naa10 and Naa15 subunits of NatA. These interactions promote catalytic crosstalk within the human complex, but do so to a lesser extent in the yeast complex, where Naa50 activity is compromised. These studies have implications for understanding the role of the NatA/Naa50 complex in modulating the majority of the N-terminal acetylome in diverse species. Structure and Mechanism of Acetylation by the N-Terminal Dual Enzyme NatA/Naa50 Complex.,Deng S, Magin RS, Wei X, Pan B, Petersson EJ, Marmorstein R Structure. 2019 May 13. pii: S0969-2126(19)30136-4. doi:, 10.1016/j.str.2019.04.014. PMID:31155310 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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