9QQA

Ternary complex of translating ribosome, NAC and NMT1

これはPDB形式変換不可エントリーです。

9QQA の概要

• エントリーDOI: 10.2210/pdb9qqa/pdb
• EMDBエントリー: 53295
• 分子名称: 18S rRNA, Small ribosomal subunit protein uS2, 40S ribosomal protein S3a, ... (92 entities in total)
• 機能のキーワード: translation, co-translational protein processing, ribosome
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 86
• 化学式量合計: 3954487.11

構造登録者

Echeverria, B.,Jaskolowski, M.,Scaiola, A.,Ban, N. (登録日: 2025-03-31, 公開日: 2025-07-16, 最終更新日: 2025-07-23)

主引用文献

Gamerdinger, M.,Echeverria, B.,Lentzsch, A.M.,Burg, N.,Fan, Z.,Jaskolowski, M.,Scaiola, A.,Piening, S.,Shan, S.O.,Ban, N.,Deuerling, E.
Mechanism of cotranslational protein N-myristoylation in human cells.
Mol.Cell, 2025

PubMed Abstract: N-myristoyltransferases (NMTs) cotranslationally transfer the fatty acid myristic acid to the N terminus of newly synthesized proteins, regulating their function and cellular localization. These enzymes are important drug targets for the treatment of cancer and viral infections. N-myristoylation of nascent proteins occurs specifically on N-terminal glycine residues after the excision of the initiator methionine by methionine aminopeptidases (METAPs). How NMTs interact with ribosomes and gain timely and specific access to their substrates remains unknown. Here, we show that human NMT1 exchanges with METAP1 at the ribosomal tunnel exit to form an active cotranslational complex together with the nascent polypeptide-associated complex (NAC). NMT1 binding is sequence selective and specifically triggered by methionine excision, which exposes the N-myristoylation motif in the nascent chain. The revealed mode of interaction of NMT1 with NAC and the methionine-cleaved nascent protein elucidates how a specific subset of proteins can be efficiently N-myristoylated in human cells.

PubMed: 40639378
DOI: 10.1016/j.molcel.2025.06.015

実験手法

ELECTRON MICROSCOPY (2.8 Å)