2rfo
From Proteopedia
(Difference between revisions)
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<StructureSection load='2rfo' size='340' side='right'caption='[[2rfo]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='2rfo' size='340' side='right'caption='[[2rfo]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[2rfo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2rfo]] is a 2 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=2RFO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RFO FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2rfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rfo OCA], [https://pdbe.org/2rfo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rfo RCSB], [https://www.ebi.ac.uk/pdbsum/2rfo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rfo 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=2rfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rfo OCA], [https://pdbe.org/2rfo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rfo RCSB], [https://www.ebi.ac.uk/pdbsum/2rfo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rfo ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
- | + | [https://www.uniprot.org/uniprot/NIC96_YEAST NIC96_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. NIC96, which is localized to the core of the NPC and the distal ring of the nuclear basket, is required for de novo assembly of NPCs. It is involved in nuclear GSP1 import.<ref>PMID:7828598</ref> <ref>PMID:8682855</ref> <ref>PMID:9017593</ref> <ref>PMID:10428845</ref> <ref>PMID:10617624</ref> <ref>PMID:11121302</ref> <ref>PMID:10806080</ref> <ref>PMID:11689687</ref> <ref>PMID:12403813</ref> <ref>PMID:12496130</ref> <ref>PMID:12730220</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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=2rfo ConSurf]. | </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=2rfo ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | Nic96 is a conserved nucleoporin that recruits the Nsp1-Nup49-Nup57 complex, a module with Phe-Gly (FG) repeats, to the central transport channel of the nuclear pore complex (NPC). Nic96 binds the Nsp1 complex via its N domain and assembles into the NPC framework via its central and C domain. Here, we report the crystal structure of a large structural nucleoporin, Nic96 without its N domain (Nic96DeltaN). Nic96DeltaN is composed of three domains and is a straight molecule that--although almost entirely helical--exhibits strong deviations from the predicted alpha-solenoid fold. The missing N domain projects midway from the Nic96 molecule, indicating how the Nsp1 complex might be located with respect to the rod-like Nic96. Notably, Nic96DeltaN binds in vitro to FG repeats of the Nsp1 complex. These data suggest a model of how Nic96 could organize a transport module with coiled-coil domains and FG repeats in the central pore channel. | ||
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- | Structural basis of the nic96 subcomplex organization in the nuclear pore channel.,Schrader N, Stelter P, Flemming D, Kunze R, Hurt E, Vetter IR Mol Cell. 2008 Jan 18;29(1):46-55. PMID:18206968<ref>PMID:18206968</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 2rfo" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: Atcc 18824]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Flemming | + | [[Category: Saccharomyces cerevisiae]] |
- | [[Category: Hurt | + | [[Category: Flemming D]] |
- | [[Category: Kunze | + | [[Category: Hurt E]] |
- | [[Category: Schrader | + | [[Category: Kunze K]] |
- | [[Category: Stelter | + | [[Category: Schrader N]] |
- | [[Category: Vetter | + | [[Category: Stelter P]] |
- | + | [[Category: Vetter IR]] | |
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Current revision
Crystral Structure of the nucleoporin Nic96
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