9I2D

NMT1-NAC bound human RNC with 10 amino acid ARF1-linker

これはPDB形式変換不可エントリーです。

9I2D の概要

• エントリーDOI: 10.2210/pdb9i2d/pdb
• EMDBエントリー: 52581
• 分子名称: CMV-staller mRNA with 18aa ARF1-linker, 60S ribosomal protein L4, 60S ribosomal protein L5, ... (91 entities in total)
• 機能のキーワード: myristoylation, nmt1, co-translational, nac, ribosome, rnc
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 88
• 化学式量合計: 4154063.19

構造登録者

Denk, T.,Berninghausen, O.,Beckmann, R. (登録日: 2025-01-20, 公開日: 2026-02-04, 最終更新日: 2026-02-18)

主引用文献

Denk, T.,Monassa, P.,Musial, J.,Berninghausen, O.,Beatrix, B.,Giglione, C.,Meinnel, T.,Beckmann, R.
Structural basis of co-translational N-myristoylation in humans.
Nat Commun, 17:1191-1191, 2026

PubMed Abstract: Modifications of proteins occurring during translation are critical for protein localization, stability and function. N-myristoylation is an essential N-terminal lipid modification catalyzed co-translationally by N-myristoyltransferases (NMTs) which have been identified as promising drug targets. However, its molecular basis in the context of the translating ribosome is not known. Here, we reveal the structural basis for co-translational N-myristoylation by NMT1 on the human ribosome by cryo-electron microscopy (cryo-EM). We show that NMT1 binds near the peptide tunnel exit and interacts with the nascent polypeptide-associated complex (NAC). Unlike other multi-enzyme complexes that act simultaneously, we find that methionine excision by methionine aminopeptidases and N-myristoylation occur sequentially via consecutive binding to the ribosome. Furthermore, our data suggest that NMT1 remains associated with elongating nascent chains, indicating a co-translational chaperone-like function in partnership with NAC. These insights provide a molecular foundation for the understanding of the co-translational N-myristoylation mechanism in humans.

PubMed: 41577716
DOI: 10.1038/s41467-025-67962-4

実験手法

ELECTRON MICROSCOPY (2.19 Å)