4KVX

Crystal structure of Naa10 (Ard1) bound to AcCoA

Summary for 4KVX

• Entry DOI: 10.2210/pdb4kvx/pdb
• Related: 4KVM 4KVO
• Descriptor: N-terminal acetyltransferase A complex catalytic subunit ard1, ACETYL COENZYME *A (3 entities in total)
• Functional Keywords: acetyltransferase, transferase
• Biological source: Schizosaccharomyces pombe (Fission yeast)
• Cellular location: Cytoplasm: Q9UTI3
• Total number of polymer chains: 2
• Total formula weight: 38524.76

Authors

Liszczak, G.P.,Marmorstein, R.Q. (deposition date: 2013-05-23, release date: 2013-07-31, Last modification date: 2024-10-30)

Primary citation

Liszczak, G.,Goldberg, J.M.,Foyn, H.,Petersson, E.J.,Arnesen, T.,Marmorstein, R.
Molecular basis for N-terminal acetylation by the heterodimeric NatA complex.
Nat.Struct.Mol.Biol., 20:1098-1105, 2013

PubMed Abstract: N-terminal acetylation is ubiquitous among eukaryotic proteins and controls a myriad of biological processes. Of the N-terminal acetyltransferases (NATs) that facilitate this cotranslational modification, the heterodimeric NatA complex has the most diversity for substrate selection and modifies the majority of all N-terminally acetylated proteins. Here, we report the X-ray crystal structure of the 100-kDa holo-NatA complex from Schizosaccharomyces pombe, in the absence and presence of a bisubstrate peptide-CoA-conjugate inhibitor, as well as the structure of the uncomplexed Naa10p catalytic subunit. The NatA-Naa15p auxiliary subunit contains 13 tetratricopeptide motifs and adopts a ring-like topology that wraps around the NatA-Naa10p subunit, an interaction that alters the Naa10p active site for substrate-specific acetylation. These studies have implications for understanding the mechanistic details of other NAT complexes and how regulatory subunits modulate the activity of the broader family of protein acetyltransferases.

PubMed: 23912279
DOI: 10.1038/nsmb.2636

Experimental method

X-RAY DIFFRACTION (2 Å)