7OJU

Chaetomium thermophilum Naa50 GNAT-domain in complex with bisubstrate analogue CoA-Ac-MVNAL

7OJU の概要

• エントリーDOI: 10.2210/pdb7oju/pdb
• 関連するPDBエントリー: 7OJV
• 分子名称: N-acetyltransferase-like protein, MVNAL Peptide, GLYCEROL, ... (6 entities in total)
• 機能のキーワード: n-alpha-acetyltransferase, gnat-fold, naa50, chaetomium thermophilum, transferase
• 由来する生物種: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 25847.10

構造登録者

Weidenhausen, J.,Kopp, J.,Sinning, I. (登録日: 2021-05-17, 公開日: 2022-09-28, 最終更新日: 2024-10-16)

主引用文献

Weidenhausen, J.,Kopp, J.,Ruger-Herreros, C.,Stein, F.,Haberkant, P.,Lapouge, K.,Sinning, I.
Extended N-Terminal Acetyltransferase Naa50 in Filamentous Fungi Adds to Naa50 Diversity.
Int J Mol Sci, 23:-, 2022

PubMed Abstract: Most eukaryotic proteins are N-terminally acetylated by a set of Nα acetyltransferases (NATs). This ancient and ubiquitous modification plays a fundamental role in protein homeostasis, while mutations are linked to human diseases and phenotypic defects. In particular, Naa50 features species-specific differences, as it is inactive in yeast but active in higher eukaryotes. Together with NatA, it engages in NatE complex formation for cotranslational acetylation. Here, we report Naa50 homologs from the filamentous fungi and with significant N- and C-terminal extensions to the conserved GNAT domain. Structural and biochemical analyses show that Naa50 shares the GNAT structure and substrate specificity with other homologs. However, in contrast to previously analyzed Naa50 proteins, it does not form NatE. The elongated N-terminus increases Naa50 thermostability and binds to dynein light chain protein 1, while our data suggest that conserved positive patches in the C-terminus allow for ribosome binding independent of NatA. Our study provides new insights into the many facets of Naa50 and highlights the diversification of NATs during evolution.

PubMed: 36142717
DOI: 10.3390/ijms231810805

実験手法

X-RAY DIFFRACTION (1.1 Å)