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'''X-RAY STRUCTURE OF THE RNA-BINDING PROTEIN SHE2p''' | '''X-RAY STRUCTURE OF THE RNA-BINDING PROTEIN SHE2p''' | ||
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[[Category: Singer, R H.]] | [[Category: Singer, R H.]] | ||
[[Category: Zenklusen, D.]] | [[Category: Zenklusen, D.]] | ||
[[Category: | [[Category: Basic helical hairpin]] | ||
[[Category: | [[Category: Dimer]] | ||
[[Category: | [[Category: Five helix bundle]] | ||
[[Category: | [[Category: Rna-binding protein]] | ||
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Revision as of 12:11, 3 May 2008
X-RAY STRUCTURE OF THE RNA-BINDING PROTEIN SHE2p
Overview
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.
About this Structure
1XLY is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
She2p is a novel RNA binding protein with a basic helical hairpin motif., Niessing D, Huttelmaier S, Zenklusen D, Singer RH, Burley SK, Cell. 2004 Nov 12;119(4):491-502. PMID:15537539 Page seeded by OCA on Sat May 3 15:11:57 2008
