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5M0I

Crystal structure of the nuclear complex with She2p and the ASH1 mRNA E3-localization element

Summary for 5M0I
Entry DOI10.2210/pdb5m0i/pdb
Related5M0H
DescriptorSWI5-dependent HO expression protein 2, ASH1-E3 element, RNA (28-MER), SWI5-dependent HO expression protein 3, ... (7 entities in total)
Functional Keywordsshe2p, ash1-mrna, mrna transport, transport protein
Biological sourceSaccharomyces cerevisiae
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Cellular locationCytoplasm : B3LQW9
Endoplasmic reticulum membrane ; Peripheral membrane protein : P38272
Total number of polymer chains9
Total formula weight138890.91
Authors
Edelmann, F.T.,Janowski, R.,Niessing, D. (deposition date: 2016-10-05, release date: 2017-01-18, Last modification date: 2024-01-17)
Primary citationEdelmann, F.T.,Schlundt, A.,Heym, R.G.,Jenner, A.,Niedner-Boblenz, A.,Syed, M.I.,Paillart, J.C.,Stehle, R.,Janowski, R.,Sattler, M.,Jansen, R.P.,Niessing, D.
Molecular architecture and dynamics of ASH1 mRNA recognition by its mRNA-transport complex.
Nat. Struct. Mol. Biol., 24:152-161, 2017
Cited by
PubMed Abstract: mRNA localization is an essential mechanism of gene regulation and is required for processes such as stem-cell division, embryogenesis and neuronal plasticity. It is not known which features in the cis-acting mRNA localization elements (LEs) are specifically recognized by motor-containing transport complexes. To the best of our knowledge, no high-resolution structure is available for any LE in complex with its cognate protein complex. Using X-ray crystallography and complementary techniques, we carried out a detailed assessment of an LE of the ASH1 mRNA from yeast, its complex with its shuttling RNA-binding protein She2p, and its highly specific, cytoplasmic complex with She3p. Although the RNA alone formed a flexible stem loop, She2p binding induced marked conformational changes. However, only joining by the unstructured She3p resulted in specific RNA recognition. The notable RNA rearrangements and joint action of a globular and an unfolded RNA-binding protein offer unprecedented insights into the step-wise maturation of an mRNA-transport complex.
PubMed: 28092367
DOI: 10.1038/nsmb.3351
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.41 Å)
Structure validation

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数据于2025-07-23公开中

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