1xly: Difference between revisions
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[[Image:1xly.gif|left|200px]] | [[Image:1xly.gif|left|200px]] | ||
'''X-RAY STRUCTURE OF THE RNA-BINDING PROTEIN SHE2p''' | {{Structure | ||
|PDB= 1xly |SIZE=350|CAPTION= <scene name='initialview01'>1xly</scene>, resolution 1.95Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= SHE2, YKL130C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | |||
}} | |||
'''X-RAY STRUCTURE OF THE RNA-BINDING PROTEIN SHE2p''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1XLY is a [ | 1XLY is a [[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== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15537539 15537539] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: rna-binding protein]] | [[Category: rna-binding protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:11:36 2008'' | ||
Revision as of 16:11, 20 March 2008
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| , resolution 1.95Å | |||||||
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| Gene: | SHE2, YKL130C (Saccharomyces cerevisiae) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
X-RAY STRUCTURE OF THE RNA-BINDING PROTEIN SHE2p
OverviewOverview
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 StructureAbout this Structure
1XLY is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
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
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