Cryo-EM structure of the ribosome-NatA complexCryo-EM structure of the ribosome-NatA complex

Structural highlights

6hd5 is a 3 chain structure with sequence from Saccharomyces cerevisiae (strain atcc 204508 / s288c). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Activity:N-terminal amino-acid N(alpha)-acetyltransferase NatA, with EC number 2.3.1.255
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[NAT1_YEAST] Non-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. NAT1 anchors ARD1 and NAT5 to the ribosome and may present the N termini of nascent polypeptides for acetylation.[1] [2] [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.[3]

References

  1. 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
  2. Gautschi M, Just S, Mun A, Ross S, Rucknagel P, Dubaquie Y, Ehrenhofer-Murray A, Rospert S. The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides. Mol Cell Biol. 2003 Oct;23(20):7403-14. PMID:14517307
  3. 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

6hd5, resolution 4.80Å

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