2x1g: Difference between revisions

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New page: '''Unreleased structure''' The entry 2x1g is ON HOLD until sometime in the future Authors: Bono, F., Cook, A., Gruenwald, M., Ebert, J., Conti, E. Description: Crystal structure of Imp...
 
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'''Unreleased structure'''


The entry 2x1g is ON HOLD  until sometime in the future
==Crystal structure of Importin13 - Mago-Y14 complex==
<StructureSection load='2x1g' size='340' side='right'caption='[[2x1g]], [[Resolution|resolution]] 3.35&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2x1g]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X1G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X1G 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]] 3.35&#8491;</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=2x1g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x1g OCA], [https://pdbe.org/2x1g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x1g RCSB], [https://www.ebi.ac.uk/pdbsum/2x1g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x1g ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MGN_DROME MGN_DROME] Participates in the bidirectional intercellular signaling between the posterior follicle cells and oocyte to establish spatial coordinates that induces axis formation. Complex with tsu is essential for cytoplasmic localization of oskar in the posterior pole of oocytes. Required for the polarization of the oocyte microtubule cytoskeleton.<ref>PMID:8026338</ref> <ref>PMID:9272960</ref> <ref>PMID:9210377</ref> <ref>PMID:12730685</ref>
== 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/x1/2x1g_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2x1g ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Mago and Y14 are core components of the exon junction complex (EJC), an assembly central to nonsense-mediated mRNA decay in humans and mRNA localization in flies. The Mago-Y14 heterodimer shuttles between the nucleus, where it is loaded onto specific mRNAs, and the cytoplasm, where it functions in translational regulation. The heterodimer is imported back into the nucleus by Importin 13 (Imp13), a member of the karyopherin-beta family of transport factors. We have elucidated the structural basis of the Mago-Y14 nuclear import cycle. The 3.35 A structure of the Drosophila Imp13-Mago-Y14 complex shows that Imp13 forms a ring-like molecule, reminiscent of Crm1, and encircles the Mago-Y14 cargo with a conserved interaction surface. The 2.8 A structure of human Imp13 bound to RanGTP reveals how Mago-Y14 is released in the nucleus by a steric hindrance mechanism. Comparison of the two structures suggests how this unusual karyopherin might function in bidirectional nucleocytoplasmic transport.


Authors: Bono, F., Cook, A., Gruenwald, M., Ebert, J., Conti, E.
Nuclear import mechanism of the EJC component Mago-Y14 revealed by structural studies of importin 13.,Bono F, Cook AG, Grunwald M, Ebert J, Conti E Mol Cell. 2010 Jan 29;37(2):211-22. PMID:20122403<ref>PMID:20122403</ref>


Description: Crystal structure of Importin13 -Mago-Y14 complex
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 13 13:28:35 2010''
<div class="pdbe-citations 2x1g" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Large Structures]]
[[Category: Bono F]]
[[Category: Conti E]]
[[Category: Cook AG]]
[[Category: Ebert J]]
[[Category: Gruenwald M]]

Latest revision as of 13:21, 20 December 2023

Crystal structure of Importin13 - Mago-Y14 complexCrystal structure of Importin13 - Mago-Y14 complex

Structural highlights

2x1g is a 6 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.35Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MGN_DROME Participates in the bidirectional intercellular signaling between the posterior follicle cells and oocyte to establish spatial coordinates that induces axis formation. Complex with tsu is essential for cytoplasmic localization of oskar in the posterior pole of oocytes. Required for the polarization of the oocyte microtubule cytoskeleton.[1] [2] [3] [4]

Evolutionary Conservation

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

Publication Abstract from PubMed

Mago and Y14 are core components of the exon junction complex (EJC), an assembly central to nonsense-mediated mRNA decay in humans and mRNA localization in flies. The Mago-Y14 heterodimer shuttles between the nucleus, where it is loaded onto specific mRNAs, and the cytoplasm, where it functions in translational regulation. The heterodimer is imported back into the nucleus by Importin 13 (Imp13), a member of the karyopherin-beta family of transport factors. We have elucidated the structural basis of the Mago-Y14 nuclear import cycle. The 3.35 A structure of the Drosophila Imp13-Mago-Y14 complex shows that Imp13 forms a ring-like molecule, reminiscent of Crm1, and encircles the Mago-Y14 cargo with a conserved interaction surface. The 2.8 A structure of human Imp13 bound to RanGTP reveals how Mago-Y14 is released in the nucleus by a steric hindrance mechanism. Comparison of the two structures suggests how this unusual karyopherin might function in bidirectional nucleocytoplasmic transport.

Nuclear import mechanism of the EJC component Mago-Y14 revealed by structural studies of importin 13.,Bono F, Cook AG, Grunwald M, Ebert J, Conti E Mol Cell. 2010 Jan 29;37(2):211-22. PMID:20122403[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Newmark PA, Boswell RE. The mago nashi locus encodes an essential product required for germ plasm assembly in Drosophila. Development. 1994 May;120(5):1303-13. PMID:8026338
  2. ↑ Newmark PA, Mohr SE, Gong L, Boswell RE. mago nashi mediates the posterior follicle cell-to-oocyte signal to organize axis formation in Drosophila. Development. 1997 Aug;124(16):3197-207. PMID:9272960
  3. ↑ Micklem DR, Dasgupta R, Elliott H, Gergely F, Davidson C, Brand A, Gonzalez-Reyes A, St Johnston D. The mago nashi gene is required for the polarisation of the oocyte and the formation of perpendicular axes in Drosophila. Curr Biol. 1997 Jul 1;7(7):468-78. PMID:9210377
  4. ↑ Fribourg S, Gatfield D, Izaurralde E, Conti E. A novel mode of RBD-protein recognition in the Y14-Mago complex. Nat Struct Biol. 2003 Jun;10(6):433-9. PMID:12730685 doi:10.1038/nsb926
  5. ↑ Bono F, Cook AG, Grunwald M, Ebert J, Conti E. Nuclear import mechanism of the EJC component Mago-Y14 revealed by structural studies of importin 13. Mol Cell. 2010 Jan 29;37(2):211-22. PMID:20122403 doi:10.1016/j.molcel.2010.01.007

2x1g, resolution 3.35Å

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