8S6U

Structure of MLLE domain of Pab1 in complex with PAM2 of Upa1

8S6U の概要

• エントリーDOI: 10.2210/pdb8s6u/pdb
• 関連するPDBエントリー: 8S6N
• 分子名称: Polyadenylate-binding protein 1, FYVE zinc finger domain protein UPA1 (3 entities in total)
• 機能のキーワード: rna transport, rna binding protein
• 由来する生物種: Ustilago maydis; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 18286.67

構造登録者

Devan, S.,Shanmugasundaram, S.,Muentjes, K.,Smits, S.H.,Altegoer, F.,Feldbruegge, M. (登録日: 2024-02-28, 公開日: 2024-10-30, 最終更新日: 2024-11-20)

主引用文献

Devan, S.K.,Shanmugasundaram, S.,Muntjes, K.,Postma, J.,Smits, S.H.J.,Altegoer, F.,Feldbrugge, M.
Deciphering the RNA-binding protein network during endosomal mRNA transport.
Proc.Natl.Acad.Sci.USA, 121:e2404091121-e2404091121, 2024

PubMed Abstract: Microtubule-dependent endosomal transport is crucial for polar growth, ensuring the precise distribution of cellular cargos such as proteins and mRNAs. However, the molecular mechanism linking mRNAs to the endosomal surface remains poorly understood. Here, we present a structural analysis of the key RNA-binding protein Rrm4 from . Our findings reveal a different type of MademoiseLLE domain (MLLE) featuring a seven-helical bundle that provides a distinct binding interface. A comparative analysis with the canonical MademoiseLLE domain of the poly(A)-binding protein Pab1 disclosed unique characteristics of both domains. Deciphering the MLLE binding code enabled prediction and verification of previously unknown Rrm4 interactors containing short linear motifs. Importantly, we demonstrated that the human MLLE domains, such as those of PABPC1 and UBR5, employed a similar principle to distinguish among interaction partners. Thus, our study provides detailed mechanistic insights into how structural variations in the widely distributed MLLE domain facilitate mRNA attachment during endosomal transport.

PubMed: 39499630
DOI: 10.1073/pnas.2404091121

実験手法

X-RAY DIFFRACTION (2 Å)