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8S6U

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

Summary for 8S6U
Entry DOI10.2210/pdb8s6u/pdb
Related8S6N
DescriptorPolyadenylate-binding protein 1, FYVE zinc finger domain protein UPA1 (3 entities in total)
Functional Keywordsrna transport, rna binding protein
Biological sourceUstilago maydis
More
Total number of polymer chains4
Total formula weight18286.67
Authors
Devan, S.,Shanmugasundaram, S.,Muentjes, K.,Smits, S.H.,Altegoer, F.,Feldbruegge, M. (deposition date: 2024-02-28, release date: 2024-10-30, Last modification date: 2024-11-20)
Primary citationDevan, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

237735

数据于2025-06-18公开中

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