1xly: Difference between revisions

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==X-RAY STRUCTURE OF THE RNA-BINDING PROTEIN SHE2p==
==X-RAY STRUCTURE OF THE RNA-BINDING PROTEIN SHE2p==
<StructureSection load='1xly' size='340' side='right'caption='[[1xly]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
<StructureSection load='1xly' size='340' side='right'caption='[[1xly]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1xly]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XLY OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1XLY FirstGlance]. <br>
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XLY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XLY FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SHE2, YKL130C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xly FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xly OCA], [https://pdbe.org/1xly PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xly RCSB], [https://www.ebi.ac.uk/pdbsum/1xly PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xly ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1xly FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xly OCA], [http://pdbe.org/1xly PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xly RCSB], [http://www.ebi.ac.uk/pdbsum/1xly PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xly ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/SHE2_YEAST SHE2_YEAST]] RNA-binding protein that binds specific mRNAs including the ASH1 mRNA, coding for a repressor of the HO endonuclease. Part of the mRNA localization machinery that restricts accumulation of certain proteins to the bud and in the daughter cell. Recruits the MYO4-SHE3 complex to the ASH1 mRNA. Recruites also LOC1 and PUF6 to ASH1 mRNA, which are required for translational repression of this mRNA.<ref>PMID:10212145</ref> <ref>PMID:10359695</ref> <ref>PMID:11032818</ref> <ref>PMID:11101531</ref> <ref>PMID:12499354</ref> <ref>PMID:13679573</ref> <ref>PMID:14561888</ref> <ref>PMID:14691136</ref> <ref>PMID:15328357</ref> <ref>PMID:15537539</ref> <ref>PMID:15899876</ref> <ref>PMID:16890529</ref> <ref>PMID:18566598</ref> <ref>PMID:19244342</ref> <ref>PMID:20713510</ref> <ref>PMID:9809065</ref> 
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1xly ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1xly ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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<ref>PMID:15537539</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1xly" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 18824]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Burley, S K]]
[[Category: Burley SK]]
[[Category: Huettelmaier, S]]
[[Category: Huettelmaier S]]
[[Category: Niessing, D]]
[[Category: Niessing D]]
[[Category: Singer, R H]]
[[Category: Singer RH]]
[[Category: Zenklusen, D]]
[[Category: Zenklusen D]]
[[Category: Basic helical hairpin]]
[[Category: Dimer]]
[[Category: Five helix bundle]]
[[Category: Rna binding protein]]
[[Category: Rna-binding protein]]

Revision as of 19:42, 20 October 2021

X-RAY STRUCTURE OF THE RNA-BINDING PROTEIN SHE2pX-RAY STRUCTURE OF THE RNA-BINDING PROTEIN SHE2p

Structural highlights

Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Drag the structure with the mouse to rotate

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