6O07

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

Summary for 6O07

• Entry DOI: 10.2210/pdb6o07/pdb
• Descriptor: N-terminal acetyltransferase A complex subunit NAT5, Naa15, N-terminal acetyltransferase A complex catalytic subunit ARD1, ... (10 entities in total)
• Functional Keywords: n-terminal acetylation, protein complex, nata, naa50, nate, transferase
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Total number of polymer chains: 3
• Total formula weight: 149947.08

Authors

Deng, S.,Marmorstein, R. (deposition date: 2019-02-15, release date: 2019-06-12, Last modification date: 2023-10-11)

Primary citation

Deng, S.,Magin, R.S.,Wei, X.,Pan, B.,Petersson, E.J.,Marmorstein, R.
Structure and Mechanism of Acetylation by the N-Terminal Dual Enzyme NatA/Naa50 Complex.
Structure, 27:1057-, 2019

PubMed Abstract: 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.

PubMed: 31155310
DOI: 10.1016/j.str.2019.04.014

Experimental method

X-RAY DIFFRACTION (2.702 Å)