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==Crystal structure of the Chaetomium thermophilum heterotrimeric Nup82 NTD-Nup159 TAIL-Nup145N APD complex==
==Crystal structure of the Chaetomium thermophilum heterotrimeric Nup82 NTD-Nup159 TAIL-Nup145N APD complex==
<StructureSection load='5cww' size='340' side='right' caption='[[5cww]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='5cww' size='340' side='right'caption='[[5cww]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5cww]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CWW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CWW FirstGlance]. <br>
<table><tr><td colspan='2'>[[5cww]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetomium_thermophilum_var._thermophilum_DSM_1495 Chaetomium thermophilum var. thermophilum DSM 1495]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CWW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CWW FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5cwt|5cwt]], [[5cwu|5cwu]], [[5cwv|5cwv]], [[5cws|5cws]]</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]] 2.2&#8491;</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=5cww FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cww OCA], [http://pdbe.org/5cww PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cww RCSB], [http://www.ebi.ac.uk/pdbsum/5cww 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=5cww FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cww OCA], [https://pdbe.org/5cww PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cww RCSB], [https://www.ebi.ac.uk/pdbsum/5cww PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cww ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/NU145_CHATD NU145_CHATD]] 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. NUP145 is autocatalytically cleaved in vivo in 2 polypeptides which assume different functions in the NPC. NUP145N as one of the FG repeat nucleoporins participates in karyopherin interactions and contains part of the autocatalytic cleavage activity. NUP145C as part of the NUP84 complex is involved in nuclear poly(A)+ RNA and tRNA export.[UniProtKB:P49687] [[http://www.uniprot.org/uniprot/NU159_CHATD NU159_CHATD]] 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.[UniProtKB:P40477] [[http://www.uniprot.org/uniprot/NUP82_CHATD NUP82_CHATD]] 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.[UniProtKB:P40368]
[https://www.uniprot.org/uniprot/NU145_CHATD NU145_CHATD] 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. NUP145 is autocatalytically cleaved in vivo in 2 polypeptides which assume different functions in the NPC. NUP145N as one of the FG repeat nucleoporins participates in karyopherin interactions and contains part of the autocatalytic cleavage activity. NUP145C as part of the NUP84 complex is involved in nuclear poly(A)+ RNA and tRNA export.[UniProtKB:P49687]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The nuclear pore complex (NPC) constitutes the sole gateway for bidirectional nucleocytoplasmic transport. We present the reconstitution and interdisciplinary analyses of the ~425-kDa inner ring complex (IRC), which forms the central transport channel and diffusion barrier of the NPC, revealing its interaction network and equimolar stoichiometry. The Nsp1*Nup49*Nup57 channel nucleoporin hetero-trimer (CNT) attaches to the IRC solely through the adaptor nucleoporin Nic96. The CNT*Nic96 structure reveals that Nic96 functions as an assembly sensor that recognizes the three dimensional architecture of the CNT, thereby mediating the incorporation of a defined CNT state into the NPC. We propose that the IRC adopts a relatively rigid scaffold that recruits the CNT to primarily form the diffusion barrier of the NPC, rather than enabling channel dilation.
 
Architecture of the fungal nuclear pore inner ring complex.,Stuwe T, Bley CJ, Thierbach K, Petrovic S, Schilbach S, Mayo DJ, Perriches T, Rundlet EJ, Jeon YE, Collins LN, Huber FM, Lin DH, Paduch M, Koide A, Lu V, Fischer J, Hurt E, Koide S, Kossiakoff AA, Hoelz A Science. 2015 Aug 27. pii: aac9176. PMID:26316600<ref>PMID:26316600</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
==See Also==
</div>
*[[Nucleoporin 3D structures|Nucleoporin 3D structures]]
<div class="pdbe-citations 5cww" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bley, C J]]
[[Category: Chaetomium thermophilum var. thermophilum DSM 1495]]
[[Category: Collins, L N]]
[[Category: Large Structures]]
[[Category: Fischer, J]]
[[Category: Bley CJ]]
[[Category: Hoelz, A]]
[[Category: Collins LN]]
[[Category: Hurt, E]]
[[Category: Fischer J]]
[[Category: Jeon, Y E]]
[[Category: Hoelz A]]
[[Category: Koide, A]]
[[Category: Hurt E]]
[[Category: Koide, S]]
[[Category: Jeon YE]]
[[Category: Kossiakoff, A A]]
[[Category: Koide A]]
[[Category: Lin, D H]]
[[Category: Koide S]]
[[Category: Lu, V]]
[[Category: Kossiakoff AA]]
[[Category: Mayo, D J]]
[[Category: Lin DH]]
[[Category: Paduch, M]]
[[Category: Lu V]]
[[Category: Perriches, T]]
[[Category: Mayo DJ]]
[[Category: Petrovic, S]]
[[Category: Paduch M]]
[[Category: Rundlet, E J]]
[[Category: Perriches T]]
[[Category: Schilbach, S]]
[[Category: Petrovic S]]
[[Category: Stuwe, T]]
[[Category: Rundlet EJ]]
[[Category: Thierbach, K]]
[[Category: Schilbach S]]
[[Category: Nucleocytoplasmic transport]]
[[Category: Stuwe T]]
[[Category: Transport protein]]
[[Category: Thierbach K]]

Latest revision as of 15:22, 6 March 2024

Crystal structure of the Chaetomium thermophilum heterotrimeric Nup82 NTD-Nup159 TAIL-Nup145N APD complexCrystal structure of the Chaetomium thermophilum heterotrimeric Nup82 NTD-Nup159 TAIL-Nup145N APD complex

Structural highlights

5cww is a 3 chain structure with sequence from Chaetomium thermophilum var. thermophilum DSM 1495. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NU145_CHATD 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. NUP145 is autocatalytically cleaved in vivo in 2 polypeptides which assume different functions in the NPC. NUP145N as one of the FG repeat nucleoporins participates in karyopherin interactions and contains part of the autocatalytic cleavage activity. NUP145C as part of the NUP84 complex is involved in nuclear poly(A)+ RNA and tRNA export.[UniProtKB:P49687]

See Also

5cww, resolution 2.20Å

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