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| | <StructureSection load='5hb7' size='340' side='right'caption='[[5hb7]], [[Resolution|resolution]] 0.82Å' scene=''> | | <StructureSection load='5hb7' size='340' side='right'caption='[[5hb7]], [[Resolution|resolution]] 0.82Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5hb7]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chatd Chatd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HB7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HB7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5hb7]] is a 1 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=5HB7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HB7 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></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]] 0.819Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5hax|5hax]], [[5hay|5hay]], [[5haz|5haz]], [[5hb1|5hb1]], [[5hb2|5hb2]], [[5hb0|5hb0]], [[5hb3|5hb3]], [[5hb4|5hb4]], [[5hb5|5hb5]], [[5hb6|5hb6]], [[5hb8|5hb8]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NUP53, CTHT_0012410 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=759272 CHATD])</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=5hb7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hb7 OCA], [https://pdbe.org/5hb7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hb7 RCSB], [https://www.ebi.ac.uk/pdbsum/5hb7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hb7 ProSAT]</span></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=5hb7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hb7 OCA], [http://pdbe.org/5hb7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hb7 RCSB], [http://www.ebi.ac.uk/pdbsum/5hb7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hb7 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/NUP53_CHATD NUP53_CHATD] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chatd]] | + | [[Category: Chaetomium thermophilum var. thermophilum DSM 1495]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hoelz, A]] | + | [[Category: Hoelz A]] |
| - | [[Category: Lin, D H]] | + | [[Category: Lin DH]] |
| - | [[Category: Stuwe, T]] | + | [[Category: Stuwe T]] |
| - | [[Category: Nucleocytoplasmic transport]]
| + | |
| - | [[Category: Protein transport]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
NUP53_CHATD
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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. Architecture of the symmetric core of the nuclear pore. Science. 2016 Apr 15;352(6283):aaf1015. doi: 10.1126/science.aaf1015. Epub 2016, Apr 14. PMID:27081075 doi:http://dx.doi.org/10.1126/science.aaf1015
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