1xly
From Proteopedia
(New page: 200px<br /><applet load="1xly" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xly, resolution 1.95Å" /> '''X-RAY STRUCTURE OF T...) |
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| - | [[Image:1xly.gif|left|200px]]<br /><applet load="1xly" size=" | + | [[Image:1xly.gif|left|200px]]<br /><applet load="1xly" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1xly, resolution 1.95Å" /> | caption="1xly, resolution 1.95Å" /> | ||
'''X-RAY STRUCTURE OF THE RNA-BINDING PROTEIN SHE2p'''<br /> | '''X-RAY STRUCTURE OF THE RNA-BINDING PROTEIN SHE2p'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Selective transport of mRNAs in ribonucleoprotein particles (mRNP) ensures | + | 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== | ==About this Structure== | ||
| - | 1XLY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http:// | + | 1XLY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XLY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Burley, S | + | [[Category: Burley, S K.]] |
[[Category: Huettelmaier, S.]] | [[Category: Huettelmaier, S.]] | ||
[[Category: Niessing, D.]] | [[Category: Niessing, D.]] | ||
| - | [[Category: Singer, R | + | [[Category: Singer, R H.]] |
[[Category: Zenklusen, D.]] | [[Category: Zenklusen, D.]] | ||
[[Category: basic helical hairpin]] | [[Category: basic helical hairpin]] | ||
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[[Category: rna-binding protein]] | [[Category: rna-binding protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:56:11 2008'' |
Revision as of 13:56, 21 February 2008
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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 Thu Feb 21 15:56:11 2008
