5hb6

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==Crystal structure of Chaetomium thermophilum Nup145N APD T994A mutant fused to Nup145C N==
==Crystal structure of Chaetomium thermophilum Nup145N APD T994A mutant fused to Nup145C N==
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<StructureSection load='5hb6' size='340' side='right' caption='[[5hb6]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
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<StructureSection load='5hb6' size='340' side='right'caption='[[5hb6]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5hb6]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HB6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HB6 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5hb6]] is a 2 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=5HB6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HB6 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5hax|5hax]], [[5hay|5hay]], [[5haz|5haz]], [[5hb2|5hb2]], [[5hb1|5hb1]], [[5hb0|5hb0]], [[5hb3|5hb3]], [[5hb4|5hb4]], [[5hb5|5hb5]], [[5hb7|5hb7]], [[5hb8|5hb8]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<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=5hb6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hb6 OCA], [http://pdbe.org/5hb6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hb6 RCSB], [http://www.ebi.ac.uk/pdbsum/5hb6 PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5hb6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hb6 OCA], [https://pdbe.org/5hb6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hb6 RCSB], [https://www.ebi.ac.uk/pdbsum/5hb6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hb6 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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]
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[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]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The nuclear pore complex (NPC) controls the transport of macromolecules between the nucleus and cytoplasm, but its molecular architecture has thus far remained poorly defined. We biochemically reconstituted NPC core protomers and elucidated the underlying protein-protein interaction network. Flexible linker sequences, rather than interactions between the structured core scaffold nucleoporins, mediate the assembly of the inner ring complex and its attachment to the NPC coat. X-ray crystallographic analysis of these scaffold nucleoporins revealed the molecular details of their interactions with the flexible linker sequences and enabled construction of full-length atomic structures. By docking these structures into the cryoelectron tomographic reconstruction of the intact human NPC and validating their placement with our nucleoporin interactome, we built a composite structure of the NPC symmetric core that contains ~320,000 residues and accounts for ~56 megadaltons of the NPC's structured mass. Our approach provides a paradigm for the structure determination of similarly complex macromolecular assemblies.
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Architecture of the symmetric core of the nuclear pore.,Lin DH, Stuwe T, Schilbach S, Rundlet EJ, Perriches T, Mobbs G, Fan Y, Thierbach K, Huber FM, Collins LN, Davenport AM, Jeon YE, Hoelz A Science. 2016 Apr 15;352(6283):aaf1015. doi: 10.1126/science.aaf1015. Epub 2016, Apr 14. PMID:27081075<ref>PMID:27081075</ref>
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==See Also==
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*[[Nucleoporin 3D structures|Nucleoporin 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5hb6" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Hoelz, A]]
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[[Category: Chaetomium thermophilum var. thermophilum DSM 1495]]
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[[Category: Lin, D H]]
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[[Category: Large Structures]]
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[[Category: Stuwe, T]]
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[[Category: Hoelz A]]
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[[Category: Nucleocytoplasmic transport]]
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[[Category: Lin DH]]
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[[Category: Protein transport]]
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[[Category: Stuwe T]]
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[[Category: Transport protein]]
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Current revision

Crystal structure of Chaetomium thermophilum Nup145N APD T994A mutant fused to Nup145C N

PDB ID 5hb6

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