6x05: Difference between revisions
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==== | ==Nup133 (aa55-481) from S. cerevisiae bound by VHH-SAN4== | ||
<StructureSection load='6x05' size='340' side='right'caption='[[6x05]]' scene=''> | <StructureSection load='6x05' size='340' side='right'caption='[[6x05]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | <table><tr><td colspan='2'>[[6x05]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C] and [https://en.wikipedia.org/wiki/Vicugna_pacos Vicugna pacos]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6X05 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6X05 FirstGlance]. <br> | ||
</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=6x05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6x05 OCA], [https://pdbe.org/6x05 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6x05 RCSB], [https://www.ebi.ac.uk/pdbsum/6x05 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6x05 ProSAT]</span></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'>[https://proteopedia.org/fgij/fg.htm?mol=6x05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6x05 OCA], [https://pdbe.org/6x05 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6x05 RCSB], [https://www.ebi.ac.uk/pdbsum/6x05 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6x05 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/NU133_YEAST NU133_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. NUP133 is involved in nuclear poly(A)+ RNA, tRNA and pre-ribosome export, in GSP1 nuclear import, in NPC assembly and distribution, as well as in nuclear envelope organization.<ref>PMID:7813444</ref> <ref>PMID:7862658</ref> <ref>PMID:8524308</ref> <ref>PMID:9049242</ref> <ref>PMID:11071906</ref> <ref>PMID:11823431</ref> <ref>PMID:12730220</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The hallmark of the eukaryotic cell is the complex endomembrane system that compartmentalizes cellular functions. Transport into and out of the nucleus occurs through the nuclear pore complex (NPC). The heptameric Nup84 or Y complex is an essential scaffolding component of the NPC. Here we report two nanobody-bound structures: the full-length Nup84-Nup133 C-terminal domain complex and the Nup133 N-terminal domain, both from S. cerevisiae. Together with previously published structures, this work enables the structural description of the entire 575 kDa Y complex from one species. The structure of Nup84-Nup133(CTD) details the high flexibility of this dimeric unit of the Y complex. Further, the Nup133(NTD) contains a structurally conserved amphipathic lipid packing sensor motif, confirmed by liposome interaction studies. The presented structures reveal important details about the function of the Y complex that affect our understanding of NPC structure and assembly. | |||
Yeast Nup84-Nup133 complex structure details flexibility and reveals conservation of the membrane anchoring ALPS motif.,Nordeen SA, Turman DL, Schwartz TU Nat Commun. 2020 Nov 27;11(1):6060. doi: 10.1038/s41467-020-19885-5. PMID:33247142<ref>PMID:33247142</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6x05" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Nucleoporin 3D structures|Nucleoporin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Saccharomyces cerevisiae S288C]] | ||
[[Category: Vicugna pacos]] | |||
[[Category: Nordeen SA]] | |||
[[Category: Schwartz TU]] | |||
Latest revision as of 17:39, 18 October 2023
Nup133 (aa55-481) from S. cerevisiae bound by VHH-SAN4Nup133 (aa55-481) from S. cerevisiae bound by VHH-SAN4
Structural highlights
FunctionNU133_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. NUP133 is involved in nuclear poly(A)+ RNA, tRNA and pre-ribosome export, in GSP1 nuclear import, in NPC assembly and distribution, as well as in nuclear envelope organization.[1] [2] [3] [4] [5] [6] [7] Publication Abstract from PubMedThe hallmark of the eukaryotic cell is the complex endomembrane system that compartmentalizes cellular functions. Transport into and out of the nucleus occurs through the nuclear pore complex (NPC). The heptameric Nup84 or Y complex is an essential scaffolding component of the NPC. Here we report two nanobody-bound structures: the full-length Nup84-Nup133 C-terminal domain complex and the Nup133 N-terminal domain, both from S. cerevisiae. Together with previously published structures, this work enables the structural description of the entire 575 kDa Y complex from one species. The structure of Nup84-Nup133(CTD) details the high flexibility of this dimeric unit of the Y complex. Further, the Nup133(NTD) contains a structurally conserved amphipathic lipid packing sensor motif, confirmed by liposome interaction studies. The presented structures reveal important details about the function of the Y complex that affect our understanding of NPC structure and assembly. Yeast Nup84-Nup133 complex structure details flexibility and reveals conservation of the membrane anchoring ALPS motif.,Nordeen SA, Turman DL, Schwartz TU Nat Commun. 2020 Nov 27;11(1):6060. doi: 10.1038/s41467-020-19885-5. PMID:33247142[8] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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