6Z00

Arabidopsis thaliana Naa50 in complex with bisubstrate analogue CoA-Ac-MVNAL

Summary for 6Z00

• Entry DOI: 10.2210/pdb6z00/pdb
• Related: 6YZZ
• Descriptor: Acyl-CoA N-acyltransferases (NAT) superfamily protein, MET-VAL-ASN-ALA-LEU, CARBOXYMETHYL COENZYME *A, ... (4 entities in total)
• Functional Keywords: n-alpha-acetyltransferase, gnat-fold, naa50, arabidopsis thaliana, transferase
• Biological source: Arabidopsis thaliana (Mouse-ear cress); More
• Total number of polymer chains: 4
• Total formula weight: 41551.04

Authors

Weidenhausen, J.,Kopp, J.,Lapouge, K.,Sinning, I. (deposition date: 2020-05-07, release date: 2020-12-30, Last modification date: 2024-10-16)

Primary citation

Weidenhausen, J.,Kopp, J.,Armbruster, L.,Wirtz, M.,Lapouge, K.,Sinning, I.
Structural and functional characterization of the N-terminal acetyltransferase Naa50.
Structure, 29:413-, 2021

PubMed Abstract: The majority of eukaryotic proteins is modified by N-terminal acetylation, which plays a fundamental role in protein homeostasis, localization, and complex formation. N-terminal acetyltransferases (NATs) mainly act co-translationally on newly synthesized proteins at the ribosomal tunnel exit. NatA is the major NAT consisting of Naa10 catalytic and Naa15 auxiliary subunits, and with Naa50 forms the NatE complex. Naa50 has recently been identified in Arabidopsis thaliana and is important for plant development and stress response regulation. Here, we determined high-resolution X-ray crystal structures of AtNaa50 in complex with AcCoA and a bisubstrate analog. We characterized its substrate specificity, determined its enzymatic parameters, and identified functionally important residues. Even though Naa50 is conserved among species, we highlight differences between Arabidopsis and yeast, where Naa50 is catalytically inactive but binds CoA conjugates. Our study provides insights into Naa50 conservation, species-specific adaptations, and serves as a basis for further studies of NATs in plants.

PubMed: 33400917
DOI: 10.1016/j.str.2020.12.004

Experimental method

X-RAY DIFFRACTION (1.42 Å)