6yzz

Arabidopsis thaliana Naa50 in complex with AcCoA

spinqualitylabelsall models 6yzz, resolution 1.79Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6yzz is a 1 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.79Å Ligands: ACO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9LFM3_ARATH Publication Abstract from PubMed 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. Structural and functional characterization of the N-terminal acetyltransferase Naa50.,Weidenhausen J, Kopp J, Armbruster L, Wirtz M, Lapouge K, Sinning I Structure. 2020 Dec 22. pii: S0969-2126(20)30471-8. doi:, 10.1016/j.str.2020.12.004. PMID:33400917 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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