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| | ==Crystal Structure of Importin Beta in an Ammonium Sulfate Condition== | | ==Crystal Structure of Importin Beta in an Ammonium Sulfate Condition== |
| - | <StructureSection load='4xri' size='340' side='right' caption='[[4xri]], [[Resolution|resolution]] 2.05Å' scene=''> | + | <StructureSection load='4xri' size='340' side='right'caption='[[4xri]], [[Resolution|resolution]] 2.05Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4xri]] 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=4XRI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XRI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4xri]] 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=4XRI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XRI FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.05Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4xrk|4xrk]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CTHT_0012280 ([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=4xri FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xri OCA], [https://pdbe.org/4xri PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xri RCSB], [https://www.ebi.ac.uk/pdbsum/4xri PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xri 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=4xri FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xri OCA], [http://pdbe.org/4xri PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xri RCSB], [http://www.ebi.ac.uk/pdbsum/4xri PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xri ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/G0S143_CHATD G0S143_CHATD] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4xri" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4xri" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Importin 3D structures|Importin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chatd]] | + | [[Category: Chaetomium thermophilum var. thermophilum DSM 1495]] |
| - | [[Category: Dickmanns, A]] | + | [[Category: Large Structures]] |
| - | [[Category: Ficner, R]] | + | [[Category: Dickmanns A]] |
| - | [[Category: Neumann, P]] | + | [[Category: Ficner R]] |
| - | [[Category: Tauchert, M J]] | + | [[Category: Neumann P]] |
| - | [[Category: Heat repeat protein]]
| + | [[Category: Tauchert MJ]] |
| - | [[Category: Highly flexible protein]]
| + | |
| - | [[Category: Importin-beta superfamily]]
| + | |
| - | [[Category: Nuclear import of various proteinaceous cargo molecule]]
| + | |
| - | [[Category: Nuclear transport]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| - | [[Category: Transport receptor]]
| + | |
| Structural highlights
Function
G0S143_CHATD
Publication Abstract from PubMed
In eukaryotic cells, the exchange of macromolecules between the nucleus and cytoplasm is highly selective and requires specialized soluble transport factors. Many of them belong to the importin-beta superfamily, the members of which share an overall superhelical structure owing to the tandem arrangement of a specific motif, the HEAT repeat. This structural organization leads to great intrinsic flexibility, which in turn is a prerequisite for the interaction with a variety of proteins and for its transport function. During the passage from the aqueous cytosol into the nucleus, the receptor passes the gated channel of the nuclear pore complex filled with a protein meshwork of unknown organization, which seems to be highly selective owing to the presence of FG-repeats, which are peptides with hydrophobic patches. Here, the structural changes of free importin-beta from a single organism, crystallized in polar (salt) or apolar (PEG) buffer conditions, are reported. This allowed analysis of the structural changes, which are attributable to the surrounding milieu and are not affected by bound interaction partners. The importin-beta structures obtained exhibit significant conformational changes and suggest an influence of the polarity of the environment, resulting in an extended conformation in the PEG condition. The significance of this observation is supported by SAXS experiments and the analysis of other crystal structures of importin-beta deposited in the Protein Data Bank.
Impact of the crystallization condition on importin-beta conformation.,Tauchert MJ, Hemonnot C, Neumann P, Koster S, Ficner R, Dickmanns A Acta Crystallogr D Struct Biol. 2016 Jun 1;72(Pt 6):705-17. doi:, 10.1107/S2059798316004940. Epub 2016 May 25. PMID:27303791[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Tauchert MJ, Hemonnot C, Neumann P, Koster S, Ficner R, Dickmanns A. Impact of the crystallization condition on importin-beta conformation. Acta Crystallogr D Struct Biol. 2016 Jun 1;72(Pt 6):705-17. doi:, 10.1107/S2059798316004940. Epub 2016 May 25. PMID:27303791 doi:http://dx.doi.org/10.1107/S2059798316004940
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