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: | , , , , , |
| 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.[1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Park EC, Szostak JW. ARD1 and NAT1 proteins form a complex that has N-terminal acetyltransferase activity. EMBO J. 1992 Jun;11(6):2087-93. PMID:1600941
- ↑ Deng S, Magin RS, Wei X, Pan B, Petersson EJ, Marmorstein R. Structure and Mechanism of Acetylation by the N-Terminal Dual Enzyme NatA/Naa50 Complex. Structure. 2019 May 13. pii: S0969-2126(19)30136-4. doi:, 10.1016/j.str.2019.04.014. PMID:31155310 doi:http://dx.doi.org/10.1016/j.str.2019.04.014
