8OO0

Chaetomium thermophilum Methionine Aminopeptidase 2 autoproteolysis product at the 80S ribosome

これはPDB形式変換不可エントリーです。

8OO0 の概要

• エントリーDOI: 10.2210/pdb8oo0/pdb
• EMDBエントリー: 17004
• 分子名称: 28S rRNA, 60S ribosomal protein L4-like protein, 60S ribosomal protein l5-like protein, ... (85 entities in total)
• 機能のキーワード: ribosome associated factor, protease, a-site, factor binding site, decoding center, protein maturation, proteostasis, nme, p67, p26, autoproteolysis, map, metap, map2, metap2, metal binding protein
• 由来する生物種: Thermochaetoides thermophila DSM 1495; 詳細
• タンパク質・核酸の鎖数: 85
• 化学式量合計: 3341843.11

構造登録者

Klein, M.A.,Wild, K.,Kisonaite, M.,Sinning, I. (登録日: 2023-04-04, 公開日: 2024-02-21)

主引用文献

Klein, M.A.,Wild, K.,Kisonaite, M.,Sinning, I.
Methionine aminopeptidase 2 and its autoproteolysis product have different binding sites on the ribosome.
Nat Commun, 15:716-716, 2024

PubMed Abstract: Excision of the initiator methionine is among the first co-translational processes that occur at the ribosome. While this crucial step in protein maturation is executed by two types of methionine aminopeptidases in eukaryotes (MAP1 and MAP2), additional roles in disease and translational regulation have drawn more attention to MAP2. Here, we report several cryo-EM structures of human and fungal MAP2 at the 80S ribosome. Irrespective of nascent chains, MAP2 can occupy the tunnel exit. On nascent chain displaying ribosomes, the MAP2-80S interaction is highly dynamic and the MAP2-specific N-terminal extension engages in stabilizing interactions with the long rRNA expansion segment ES27L. Loss of this extension by autoproteolytic cleavage impedes interactions at the tunnel, while promoting MAP2 to enter the ribosomal A-site, where it engages with crucial functional centers of translation. These findings reveal that proteolytic remodeling of MAP2 severely affects ribosome binding, and set the stage for targeted functional studies.

PubMed: 38267453
DOI: 10.1038/s41467-024-44862-7

実験手法

ELECTRON MICROSCOPY (3.1 Å)