5hb7: Difference between revisions
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==Crystal structure of Chaetomium thermophilum Nup53 RRM== | |||
<StructureSection load='5hb7' size='340' side='right' caption='[[5hb7]], [[Resolution|resolution]] 0.82Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5hb7]] is a 1 chain structure. 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> | |||
</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> | |||
<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='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]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:27081075</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5hb7" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Hoelz, A]] | [[Category: Hoelz, A]] | ||
[[Category: Lin, D H]] | |||
[[Category: Stuwe, T]] | [[Category: Stuwe, T]] | ||
[[Category: Nucleocytoplasmic transport]] | |||
[[Category: Protein transport]] | |||
[[Category: Transport protein]] | |||
Revision as of 19:32, 10 May 2016
Crystal structure of Chaetomium thermophilum Nup53 RRMCrystal structure of Chaetomium thermophilum Nup53 RRM
Structural highlights
Publication Abstract from PubMedThe 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. References
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