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New page: left|200px<br /><applet load="1xip" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xip, resolution 2.50Å" /> '''Crystal Structure of...
 
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[[Image:1xip.jpg|left|200px]]<br /><applet load="1xip" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1xip, resolution 2.50&Aring;" />
'''Crystal Structure of the N-terminal Domain of Nup159'''<br />


==Overview==
==Crystal Structure of the N-terminal Domain of Nup159==
Nuclear export of mRNA in eukaryotic cells is mediated by soluble, transport factors and components of the nuclear pore complex (NPC). The, cytoplasmically oriented nuclear pore protein Nup159 plays a critical role, in mRNA export through its conserved N-terminal domain (NTD). Here, we, report the crystal structure of the Nup159 NTD, refined to 2.5 A. The, structure reveals an unusually asymmetric seven-bladed beta-propeller that, is structurally conserved throughout eukarya. Using structure-based, conservation analysis, we have targeted specific surface residues for, mutagenesis. Residue substitutions in a conserved loop of the NTD abolish, in vitro binding to Dbp5, a DEAD box helicase required for mRNA export. In, vivo, these mutations cause Dbp5 mislocalization and block mRNA export., These findings suggest that the Nup159 NTD functions in mRNA export as a, binding platform, tethering shuttling Dbp5 molecules at the nuclear, periphery and locally concentrating this mRNA remodeling factor at the, cytoplasmic face of the NPC.
<StructureSection load='1xip' size='340' side='right'caption='[[1xip]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1xip]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XIP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XIP FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=1xip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xip OCA], [https://pdbe.org/1xip PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xip RCSB], [https://www.ebi.ac.uk/pdbsum/1xip PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xip ProSAT]</span></td></tr>
</table>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xi/1xip_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1xip ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Nuclear export of mRNA in eukaryotic cells is mediated by soluble transport factors and components of the nuclear pore complex (NPC). The cytoplasmically oriented nuclear pore protein Nup159 plays a critical role in mRNA export through its conserved N-terminal domain (NTD). Here, we report the crystal structure of the Nup159 NTD, refined to 2.5 A. The structure reveals an unusually asymmetric seven-bladed beta-propeller that is structurally conserved throughout eukarya. Using structure-based conservation analysis, we have targeted specific surface residues for mutagenesis. Residue substitutions in a conserved loop of the NTD abolish in vitro binding to Dbp5, a DEAD box helicase required for mRNA export. In vivo, these mutations cause Dbp5 mislocalization and block mRNA export. These findings suggest that the Nup159 NTD functions in mRNA export as a binding platform, tethering shuttling Dbp5 molecules at the nuclear periphery and locally concentrating this mRNA remodeling factor at the cytoplasmic face of the NPC.


==About this Structure==
The N-terminal domain of Nup159 forms a beta-propeller that functions in mRNA export by tethering the helicase Dbp5 to the nuclear pore.,Weirich CS, Erzberger JP, Berger JM, Weis K Mol Cell. 2004 Dec 3;16(5):749-60. PMID:15574330<ref>PMID:15574330</ref>
1XIP 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XIP OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
The N-terminal domain of Nup159 forms a beta-propeller that functions in mRNA export by tethering the helicase Dbp5 to the nuclear pore., Weirich CS, Erzberger JP, Berger JM, Weis K, Mol Cell. 2004 Dec 3;16(5):749-60. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15574330 15574330]
</div>
<div class="pdbe-citations 1xip" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Nucleoporin|Nucleoporin]]
*[[Nucleoporin 3D structures|Nucleoporin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Berger JM]]
[[Category: Berger, J.M.]]
[[Category: Erzberger JP]]
[[Category: Erzberger, J.P.]]
[[Category: Weirich CS]]
[[Category: Weirich, C.S.]]
[[Category: Weis K]]
[[Category: Weis, K.]]
[[Category: beta-propeller]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:06:14 2007''

Latest revision as of 00:39, 21 November 2024

Crystal Structure of the N-terminal Domain of Nup159

1xip, resolution 2.50Å

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