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| | ==rImp_alpha_B54NLS== | | ==rImp_alpha_B54NLS== |
| - | <StructureSection load='2yns' size='340' side='right' caption='[[2yns]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='2yns' size='340' side='right'caption='[[2yns]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2yns]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryza_sativa_japonica_group Oryza sativa japonica group] and [http://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YNS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YNS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2yns]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryza_sativa_Japonica_Group Oryza sativa Japonica Group] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YNS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YNS FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4b8j|4b8j]], [[4b8o|4b8o]], [[4b8p|4b8p]], [[2ynr|2ynr]], [[4ba3|4ba3]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</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=2yns FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yns OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2yns RCSB], [http://www.ebi.ac.uk/pdbsum/2yns PDBsum]</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=2yns FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yns OCA], [https://pdbe.org/2yns PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yns RCSB], [https://www.ebi.ac.uk/pdbsum/2yns PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yns ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/IMA1A_ORYSJ IMA1A_ORYSJ]] Functions in nuclear protein import. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Promotes docking of import substrates to the nuclear envelope.<ref>PMID:9727027</ref> <ref>PMID:11124253</ref> | + | [https://www.uniprot.org/uniprot/IMA1A_ORYSJ IMA1A_ORYSJ] Functions in nuclear protein import. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Promotes docking of import substrates to the nuclear envelope.<ref>PMID:9727027</ref> <ref>PMID:11124253</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 2yns" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Importin 3D structures|Importin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Oryza sativa japonica group]] | + | [[Category: Large Structures]] |
| | + | [[Category: Oryza sativa Japonica Group]] |
| | [[Category: Synthetic construct]] | | [[Category: Synthetic construct]] |
| - | [[Category: Boden, M]] | + | [[Category: Boden M]] |
| - | [[Category: Chang, C W]] | + | [[Category: Chang C-W]] |
| - | [[Category: Counago, R L.M]] | + | [[Category: Counago RLM]] |
| - | [[Category: Kobe, B]] | + | [[Category: Kobe B]] |
| - | [[Category: Williams, S J]] | + | [[Category: Williams SJ]] |
| - | [[Category: Nuclear localization signal]]
| + | |
| - | [[Category: Transport protein]]
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| Structural highlights
Function
IMA1A_ORYSJ Functions in nuclear protein import. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Promotes docking of import substrates to the nuclear envelope.[1] [2]
Publication Abstract from PubMed
In the classical nucleocytoplasmic import pathway, nuclear localization signals (NLSs) in cargo proteins are recognized by the import receptor importin-alpha. Importin-alpha has two separate NLS binding sites (the major and the minor site), both of which recognize positively charged amino acid clusters in NLSs. Little is known about the molecular basis of the unique features of the classical nuclear import pathway in plants. We determined the crystal structure of rice (Oryza sativa) importin-alpha1a at 2-A resolution. The structure reveals that the autoinhibitory mechanism mediated by the importin-beta binding domain of importin-alpha operates in plants, with NLS-mimicking sequences binding to both minor and major NLS binding sites. Consistent with yeast and mammalian proteins, rice importin-alpha binds the prototypical NLS from simian virus 40 large T-antigen preferentially at the major NLS binding site. We show that two NLSs, previously described as plant specific, bind to and are functional with plant, mammalian, and yeast importin-alpha proteins but interact with rice importin-alpha more strongly. The crystal structures of their complexes with rice importin-alpha show that they bind to the minor NLS binding site. By contrast, the crystal structures of their complexes with mouse (Mus musculus) importin-alpha show preferential binding to the major NLS binding site. Our results reveal the molecular basis of a number of features of the classical nuclear transport pathway specific to plants.
Crystal Structure of Rice Importin-alpha and Structural Basis of Its Interaction with Plant-Specific Nuclear Localization Signals.,Chang CW, Counago RL, Williams SJ, Boden M, Kobe B Plant Cell. 2012 Dec 18. PMID:23250448[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Jiang CJ, Imamoto N, Matsuki R, Yoneda Y, Yamamoto N. Functional characterization of a plant importin alpha homologue. Nuclear localization signal (NLS)-selective binding and mediation of nuclear import of nls proteins in vitro. J Biol Chem. 1998 Sep 11;273(37):24083-7. PMID:9727027
- ↑ Jiang CJ, Shoji K, Matsuki R, Baba A, Inagaki N, Ban H, Iwasaki T, Imamoto N, Yoneda Y, Deng XW, Yamamoto N. Molecular cloning of a novel importin alpha homologue from rice, by which constitutive photomorphogenic 1 (COP1) nuclear localization signal (NLS)-protein is preferentially nuclear imported. J Biol Chem. 2001 Mar 23;276(12):9322-9. Epub 2000 Dec 20. PMID:11124253 doi:http://dx.doi.org/10.1074/jbc.M006430200
- ↑ Chang CW, Counago RL, Williams SJ, Boden M, Kobe B. Crystal Structure of Rice Importin-alpha and Structural Basis of Its Interaction with Plant-Specific Nuclear Localization Signals. Plant Cell. 2012 Dec 18. PMID:23250448 doi:http://dx.doi.org/10.1105/tpc.112.104422
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