5M0H

Crystal structure of the central flexible region of ASH1 mRNA E3-localization element

Summary for 5M0H

• Entry DOI: 10.2210/pdb5m0h/pdb
• Descriptor: ASH1 E3 (42 nt-TL/TLR), SULFATE ION (3 entities in total)
• Functional Keywords: she2p, she3p, ash1-mrna, mrna transport, rna
• Biological source: Saccharomyces cerevisiae
• Total number of polymer chains: 1
• Total formula weight: 13600.14

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 citation

Edelmann, 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

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

Experimental method

X-RAY DIFFRACTION (2.65 Å)