2x1g

From Proteopedia

(Difference between revisions)

Revision as of 16:47, 3 November 2021

Crystal structure of Importin13 - Mago-Y14 complex

Structural highlights

2x1g is a 6 chain structure with sequence from Drome. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1rk8, 1oo0, 1hl6
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RBM8A_DROME] Involved in mRNA quality control via the nonsense-mediated mRNA decay (NMD) pathway. Also involved in localization of osk (oskar) mRNA in the posterior pole of oocytes via its interaction with mago.^[1] ^[2] [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.^[3] ^[4] ^[5] ^[6]

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^[7]

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

References

↑ Mohr SE, Dillon ST, Boswell RE. The RNA-binding protein Tsunagi interacts with Mago Nashi to establish polarity and localize oskar mRNA during Drosophila oogenesis. Genes Dev. 2001 Nov 1;15(21):2886-99. PMID:11691839 doi:http://dx.doi.org/10.1101/gad.927001
↑ 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
↑ 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
↑ 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
↑ 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
↑ 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
↑ 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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2x1g"

@@ Line 3: / Line 3: @@
 <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 [http://en.wikipedia.org/wiki/Drome Drome]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2X1G FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2x1g]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Drome Drome]. 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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1rk8|1rk8]], [[1oo0|1oo0]], [[1hl6|1hl6]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1rk8|1rk8]], [[1oo0|1oo0]], [[1hl6|1hl6]]</div></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2x1g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x1g OCA], [http://pdbe.org/2x1g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2x1g RCSB], [http://www.ebi.ac.uk/pdbsum/2x1g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2x1g ProSAT]</span></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 ==
-[[http://www.uniprot.org/uniprot/RBM8A_DROME RBM8A_DROME]] Involved in mRNA quality control via the nonsense-mediated mRNA decay (NMD) pathway. Also involved in localization of osk (oskar) mRNA in the posterior pole of oocytes via its interaction with mago.<ref>PMID:11691839</ref> <ref>PMID:12730685</ref>  [[http://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>
+[[https://www.uniprot.org/uniprot/RBM8A_DROME RBM8A_DROME]] Involved in mRNA quality control via the nonsense-mediated mRNA decay (NMD) pathway. Also involved in localization of osk (oskar) mRNA in the posterior pole of oocytes via its interaction with mago.<ref>PMID:11691839</ref> <ref>PMID:12730685</ref>  [[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]]

2x1g

From Proteopedia

Revision as of 16:47, 3 November 2021

Crystal structure of Importin13 - Mago-Y14 complex

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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