1XLY

X-RAY STRUCTURE OF THE RNA-BINDING PROTEIN SHE2p

Summary for 1XLY

• Entry DOI: 10.2210/pdb1xly/pdb
• Descriptor: SHE2p (2 entities in total)
• Functional Keywords: basic helical hairpin, five helix bundle, dimer, rna-binding protein, rna binding protein
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Total number of polymer chains: 2
• Total formula weight: 53614.50

Authors

Niessing, D.,Huettelmaier, S.,Zenklusen, D.,Singer, R.H.,Burley, S.K. (deposition date: 2004-09-30, release date: 2004-11-16, Last modification date: 2024-02-14)

Primary citation

Niessing, D.,Huettelmaier, S.,Zenklusen, D.,Singer, R.H.,Burley, S.K.
She2p is a novel RNA binding protein with a basic helical hairpin motif
Cell(Cambridge,Mass.), 119:491-502, 2004

PubMed Abstract: Selective transport of mRNAs in ribonucleoprotein particles (mRNP) ensures asymmetric distribution of information within and among eukaryotic cells. Actin-dependent transport of ASH1 mRNA in yeast represents one of the best-characterized examples of mRNP translocation. Formation of the ASH1 mRNP requires recognition of zip code elements by the RNA binding protein She2p. We determined the X-ray structure of She2p at 1.95 A resolution. She2p is a member of a previously unknown class of nucleic acid binding proteins, composed of a single globular domain with a five alpha helix bundle that forms a symmetric homodimer. After demonstrating potent, dimer-dependent RNA binding in vitro, we mapped the RNA binding surface of She2p to a basic helical hairpin in vitro and in vivo and present a mechanism for mRNA-dependent initiation of ASH1 mRNP complex assembly.

PubMed: 15537539
DOI: 10.1016/j.cell.2004.10.018

Experimental method

X-RAY DIFFRACTION (1.95 Å)