5M0I
Crystal structure of the nuclear complex with She2p and the ASH1 mRNA E3-localization element
Summary for 5M0I
Entry DOI | 10.2210/pdb5m0i/pdb |
Related | 5M0H |
Descriptor | SWI5-dependent HO expression protein 2, ASH1-E3 element, RNA (28-MER), SWI5-dependent HO expression protein 3, ... (7 entities in total) |
Functional Keywords | she2p, ash1-mrna, mrna transport, transport protein |
Biological source | Saccharomyces cerevisiae More |
Cellular location | Cytoplasm : B3LQW9 Endoplasmic reticulum membrane ; Peripheral membrane protein : P38272 |
Total number of polymer chains | 9 |
Total formula weight | 138890.91 |
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 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 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: 28092367DOI: 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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