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| | ==Structure of the yeast heterotrimeric Nup82-Nup159-Nup116 nucleoporin complex== | | ==Structure of the yeast heterotrimeric Nup82-Nup159-Nup116 nucleoporin complex== |
| - | <StructureSection load='3pbp' size='340' side='right' caption='[[3pbp]], [[Resolution|resolution]] 2.60Å' scene=''> | + | <StructureSection load='3pbp' size='340' side='right'caption='[[3pbp]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3pbp]] is a 12 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=3PBP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PBP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3pbp]] is a 12 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=3PBP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PBP FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></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]] 2.6Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NUP82, YJL061W, J1135, HRB187 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), NUP116, NSP116, YMR047C, YM9532.12C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), NUP159, NUP158, RAT7, YIL115C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=3pbp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pbp OCA], [https://pdbe.org/3pbp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pbp RCSB], [https://www.ebi.ac.uk/pdbsum/3pbp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pbp ProSAT]</span></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=3pbp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pbp OCA], [http://pdbe.org/3pbp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3pbp RCSB], [http://www.ebi.ac.uk/pdbsum/3pbp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3pbp ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/NUP82_YEAST NUP82_YEAST]] Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. It is specifically involved as part of the NUP82-NUP159-NSP1 subcomplex in nuclear mRNA and pre-ribosome export by acting as a linker tethering nucleoporins that are directly involved in nuclear transport to the NPC via its coiled-coil domain.<ref>PMID:7559750</ref> <ref>PMID:9843582</ref> <ref>PMID:10801828</ref> <ref>PMID:10891509</ref> <ref>PMID:11739405</ref> <ref>PMID:11689687</ref> [[http://www.uniprot.org/uniprot/NU159_YEAST NU159_YEAST]] Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP159 plays an important role in several nuclear export pathways including poly(A)+ RNA, pre-ribosome, and protein export.<ref>PMID:9736720</ref> <ref>PMID:9843582</ref> <ref>PMID:9891088</ref> <ref>PMID:10523319</ref> <ref>PMID:10801828</ref> <ref>PMID:10952996</ref> <ref>PMID:11387327</ref> <ref>PMID:11739405</ref> <ref>PMID:11689687</ref> <ref>PMID:12543930</ref> <ref>PMID:12604785</ref> <ref>PMID:15039779</ref> <ref>PMID:15574330</ref> [[http://www.uniprot.org/uniprot/NU116_YEAST NU116_YEAST]] Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP116 plays an important role in several nuclear export and import pathways including poly(A)+ RNA, tRNA, pre-ribosome, and protein transport.<ref>PMID:8044840</ref> <ref>PMID:8524308</ref> <ref>PMID:9463388</ref> <ref>PMID:9891088</ref> <ref>PMID:10891509</ref> <ref>PMID:10952996</ref> <ref>PMID:11071906</ref> <ref>PMID:10801828</ref> <ref>PMID:11387327</ref> <ref>PMID:11689687</ref> <ref>PMID:11104765</ref> <ref>PMID:12372823</ref> <ref>PMID:12604785</ref> <ref>PMID:15039779</ref> | + | [https://www.uniprot.org/uniprot/NUP82_YEAST NUP82_YEAST] Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. It is specifically involved as part of the NUP82-NUP159-NSP1 subcomplex in nuclear mRNA and pre-ribosome export by acting as a linker tethering nucleoporins that are directly involved in nuclear transport to the NPC via its coiled-coil domain.<ref>PMID:7559750</ref> <ref>PMID:9843582</ref> <ref>PMID:10801828</ref> <ref>PMID:10891509</ref> <ref>PMID:11739405</ref> <ref>PMID:11689687</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Nucleoporin|Nucleoporin]] | + | *[[Nucleoporin 3D structures|Nucleoporin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | + | [[Category: Large Structures]] |
| - | [[Category: Debler, E W]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Hoelz, A]] | + | [[Category: Debler EW]] |
| - | [[Category: Autoproteolysis]] | + | [[Category: Hoelz A]] |
| - | [[Category: Beta-propeller]]
| + | |
| - | [[Category: Fusion protein]]
| + | |
| - | [[Category: Mrna export]]
| + | |
| - | [[Category: Mrnp remodelling]]
| + | |
| - | [[Category: Nuclear envelope]]
| + | |
| - | [[Category: Nuclear pore complex]]
| + | |
| - | [[Category: Nucleocytoplasmic transport]]
| + | |
| - | [[Category: Nucleoporin]]
| + | |
| - | [[Category: Nucleus]]
| + | |
| - | [[Category: Oncoprotein]]
| + | |
| - | [[Category: Protein complex]]
| + | |
| - | [[Category: Protein transport]]
| + | |
| - | [[Category: Protooncogene]]
| + | |
| - | [[Category: Structural protein]]
| + | |
| - | [[Category: Translocation]]
| + | |
| - | [[Category: Transport]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
NUP82_YEAST Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. It is specifically involved as part of the NUP82-NUP159-NSP1 subcomplex in nuclear mRNA and pre-ribosome export by acting as a linker tethering nucleoporins that are directly involved in nuclear transport to the NPC via its coiled-coil domain.[1] [2] [3] [4] [5] [6]
Publication Abstract from PubMed
So far, only a few of the interactions between the approximately 30 nucleoporins comprising the modular structure of the nuclear pore complex have been defined at atomic resolution. Here we report the crystal structure, at 2.6 A resolution, of a heterotrimeric complex, composed of fragments of three cytoplasmically oriented nucleoporins of yeast: Nup82, Nup116, and Nup159. Our data show that the Nup82 fragment, representing more than the N-terminal half of the molecule, folds into an extensively decorated, seven-bladed beta-propeller that forms the centerpiece of this heterotrimeric complex and anchors both a C-terminal fragment of Nup116 and the C-terminal tail of Nup159. Binding between Nup116 and Nup82 is mutually reinforced via two loops, one emanating from the Nup82 beta-propeller and the other one from the beta-sandwich fold of Nup116, each contacting binding pockets in their counterparts. The Nup82-Nup159 interaction occurs through an amphipathic alpha-helix of Nup159, which is cradled in a large hydrophobic groove that is generated from several large surface decorations of the Nup82 beta-propeller. Although Nup159 and Nup116 fragments bind to the Nup82 beta-propeller in close vicinity, there are no direct contacts between them, consistent with the noncooperative binding that was detected biochemically. Extensive mutagenesis delineated hot-spot residues for these interactions. We also showed that the Nup82 beta-propeller binds to other yeast Nup116 family members, Nup145N, Nup100 and to the mammalian homolog, Nup98. Notably, each of the three nucleoporins contains additional nuclear pore complex binding sites, distinct from those that were defined here in the heterotrimeric Nup82*Nup159*Nup116 complex.
Structural and functional analysis of an essential nucleoporin heterotrimer on the cytoplasmic face of the nuclear pore complex.,Yoshida K, Seo HS, Debler EW, Blobel G, Hoelz A Proc Natl Acad Sci U S A. 2011 Oct 4;108(40):16571-6. Epub 2011 Sep 19. PMID:21930948[7]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Grandi P, Emig S, Weise C, Hucho F, Pohl T, Hurt EC. A novel nuclear pore protein Nup82p which specifically binds to a fraction of Nsp1p. J Cell Biol. 1995 Sep;130(6):1263-73. PMID:7559750
- ↑ Belgareh N, Snay-Hodge C, Pasteau F, Dagher S, Cole CN, Doye V. Functional characterization of a Nup159p-containing nuclear pore subcomplex. Mol Biol Cell. 1998 Dec;9(12):3475-92. PMID:9843582
- ↑ Bailer SM, Balduf C, Katahira J, Podtelejnikov A, Rollenhagen C, Mann M, Pante N, Hurt E. Nup116p associates with the Nup82p-Nsp1p-Nup159p nucleoporin complex. J Biol Chem. 2000 Aug 4;275(31):23540-8. PMID:10801828 doi:http://dx.doi.org/10.1074/jbc.M001963200
- ↑ Ho AK, Shen TX, Ryan KJ, Kiseleva E, Levy MA, Allen TD, Wente SR. Assembly and preferential localization of Nup116p on the cytoplasmic face of the nuclear pore complex by interaction with Nup82p. Mol Cell Biol. 2000 Aug;20(15):5736-48. PMID:10891509
- ↑ Gleizes PE, Noaillac-Depeyre J, Leger-Silvestre I, Teulieres F, Dauxois JY, Pommet D, Azum-Gelade MC, Gas N. Ultrastructural localization of rRNA shows defective nuclear export of preribosomes in mutants of the Nup82p complex. J Cell Biol. 2001 Dec 10;155(6):923-36. Epub 2001 Dec 10. PMID:11739405 doi:http://dx.doi.org/10.1083/jcb.200108142
- ↑ Bailer SM, Balduf C, Hurt E. The Nsp1p carboxy-terminal domain is organized into functionally distinct coiled-coil regions required for assembly of nucleoporin subcomplexes and nucleocytoplasmic transport. Mol Cell Biol. 2001 Dec;21(23):7944-55. PMID:11689687 doi:http://dx.doi.org/10.1128/MCB.21.23.7944-7955.2001
- ↑ Yoshida K, Seo HS, Debler EW, Blobel G, Hoelz A. Structural and functional analysis of an essential nucleoporin heterotrimer on the cytoplasmic face of the nuclear pore complex. Proc Natl Acad Sci U S A. 2011 Oct 4;108(40):16571-6. Epub 2011 Sep 19. PMID:21930948 doi:10.1073/pnas.1112846108
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