5c3l: Difference between revisions

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'''Unreleased structure'''


The entry 5c3l is ON HOLD  until Paper Publication
==Structure of the metazoan Nup62.Nup58.Nup54 nucleoporin complex.==
<StructureSection load='5c3l' size='340' side='right'caption='[[5c3l]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5c3l]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Camelus_dromedarius Camelus dromedarius] and [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C3L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5C3L FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</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=5c3l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c3l OCA], [https://pdbe.org/5c3l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c3l RCSB], [https://www.ebi.ac.uk/pdbsum/5c3l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c3l ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/K9ZTJ6_XENLA K9ZTJ6_XENLA]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Nuclear pore complexes (NPCs) conduct nucleocytoplasmic transport and gain transport selectivity through nucleoporin FG domains. Here, we report a structural analysis of the FG Nup62*58*54 complex, which is a crucial component of the transport system. It comprises a approximately 13 nm long trimerization interface with an unusual 2W3F coil, a canonical heterotrimeric coiled coil, and a kink that enforces a compact six-helix bundle. Nup54 also contains a ferredoxin-like domain. We further identified a heterotrimeric Nup93-binding module for NPC anchorage. The quaternary structure alternations in the Nup62 complex, which were previously proposed to trigger a general NPC-gating, are incompatible with the trimer structure. We suggest that the highly elongated Nup62 complex projects barrier-forming FG-repeats far into the central NPC channel, supporting a barrier that guards the entire cross-section.


Authors: Chug, H., Trakhanov, S., Hulsmann, B.B., Pleiner, T., Gorlich, D.
Crystal structure of the metazoan Nup62*Nup58*Nup54 nucleoporin complex.,Chug H, Trakhanov S, Hulsmann BB, Pleiner T, Gorlich D Science. 2015 Aug 20. pii: aac7420. PMID:26292704<ref>PMID:26292704</ref>


Description: Structure of the metazoan Nup62.Nup58.Nup54 nucleoporin complex.
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Chug, H]]
<div class="pdbe-citations 5c3l" style="background-color:#fffaf0;"></div>
[[Category: Hulsmann, B.B]]
 
[[Category: Gorlich, D]]
==See Also==
[[Category: Trakhanov, S]]
*[[Nucleoporin 3D structures|Nucleoporin 3D structures]]
[[Category: Pleiner, T]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Camelus dromedarius]]
[[Category: Large Structures]]
[[Category: Xenopus laevis]]
[[Category: Chug H]]
[[Category: Gorlich D]]
[[Category: Hulsmann BB]]
[[Category: Pleiner T]]
[[Category: Trakhanov S]]

Latest revision as of 14:18, 10 January 2024

Structure of the metazoan Nup62.Nup58.Nup54 nucleoporin complex.Structure of the metazoan Nup62.Nup58.Nup54 nucleoporin complex.

Structural highlights

5c3l is a 5 chain structure with sequence from Camelus dromedarius and Xenopus laevis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.9Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

K9ZTJ6_XENLA

Publication Abstract from PubMed

Nuclear pore complexes (NPCs) conduct nucleocytoplasmic transport and gain transport selectivity through nucleoporin FG domains. Here, we report a structural analysis of the FG Nup62*58*54 complex, which is a crucial component of the transport system. It comprises a approximately 13 nm long trimerization interface with an unusual 2W3F coil, a canonical heterotrimeric coiled coil, and a kink that enforces a compact six-helix bundle. Nup54 also contains a ferredoxin-like domain. We further identified a heterotrimeric Nup93-binding module for NPC anchorage. The quaternary structure alternations in the Nup62 complex, which were previously proposed to trigger a general NPC-gating, are incompatible with the trimer structure. We suggest that the highly elongated Nup62 complex projects barrier-forming FG-repeats far into the central NPC channel, supporting a barrier that guards the entire cross-section.

Crystal structure of the metazoan Nup62*Nup58*Nup54 nucleoporin complex.,Chug H, Trakhanov S, Hulsmann BB, Pleiner T, Gorlich D Science. 2015 Aug 20. pii: aac7420. PMID:26292704[1]

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

See Also

References

  1. Chug H, Trakhanov S, Hulsmann BB, Pleiner T, Gorlich D. Crystal structure of the metazoan Nup62*Nup58*Nup54 nucleoporin complex. Science. 2015 Aug 20. pii: aac7420. PMID:26292704 doi:http://dx.doi.org/10.1126/science.aac7420

5c3l, resolution 2.90Å

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