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| | <StructureSection load='5vch' size='340' side='right'caption='[[5vch]], [[Resolution|resolution]] 2.35Å' scene=''> | | <StructureSection load='5vch' size='340' side='right'caption='[[5vch]], [[Resolution|resolution]] 2.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5vch]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_56498 Atcc 56498]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VCH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VCH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5vch]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Kluyveromyces_lactis Kluyveromyces lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VCH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VCH FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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]] 2.35Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ve8|5ve8]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=5vch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vch OCA], [http://pdbe.org/5vch PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vch RCSB], [http://www.ebi.ac.uk/pdbsum/5vch PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vch ProSAT]</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=5vch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vch OCA], [https://pdbe.org/5vch PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vch RCSB], [https://www.ebi.ac.uk/pdbsum/5vch PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vch ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q6CMF0_KLULA Q6CMF0_KLULA] |
| | <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: Atcc 56498]] | + | [[Category: Kluyveromyces lactis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: An, S]] | + | [[Category: An S]] |
| - | [[Category: Cho, U S]] | + | [[Category: Cho U-S]] |
| - | [[Category: Song, J J]] | + | [[Category: Song J-J]] |
| - | [[Category: Yoon, J]] | + | [[Category: Yoon J]] |
| - | [[Category: 23 heat repeats with a right-handed superhelical solenoid structure]]
| + | |
| - | [[Category: Bidding yeast karyopherin]]
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| - | [[Category: Histone nls recognition]]
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| - | [[Category: Protein transport]]
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| - | [[Category: The extra-long helix of the repeat 23]]
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| Structural highlights
Function
Q6CMF0_KLULA
Publication Abstract from PubMed
Kap123, a major karyopherin protein of budding yeast, recognizes the nuclear localization signals (NLSs) of cytoplasmic histones H3 and H4 and translocates them into the nucleus during DNA replication. Mechanistic questions include H3- and H4-NLS redundancy toward Kap123 and the role of the conserved diacetylation of cytoplasmic H4 (K5ac and K12ac) in Kap123-mediated histone nuclear translocation. Here, we report crystal structures of full-length Kluyveromyces lactis Kap123 alone and in complex with H3- and H4-NLSs. Structures reveal the unique feature of Kap123 that possesses two discrete lysine-binding pockets for NLS recognition. Structural comparison illustrates that H3- and H4-NLSs share at least one of two lysine-binding pockets, suggesting that H3- and H4-NLSs are mutually exclusive. Additionally, acetylation of key lysine residues at NLS, particularly H4-NLS diacetylation, weakens the interaction with Kap123. These data support that cytoplasmic histone H4 diacetylation weakens the Kap123-H4-NLS interaction thereby facilitating histone Kap123-H3-dependent H3:H4/Asf1 complex nuclear translocation.
Structure-based nuclear import mechanism of histones H3 and H4 mediated by Kap123.,An S, Yoon J, Kim H, Song JJ, Cho US Elife. 2017 Oct 16;6. pii: e30244. doi: 10.7554/eLife.30244. PMID:29035199[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ An S, Yoon J, Kim H, Song JJ, Cho US. Structure-based nuclear import mechanism of histones H3 and H4 mediated by Kap123. Elife. 2017 Oct 16;6. pii: e30244. doi: 10.7554/eLife.30244. PMID:29035199 doi:http://dx.doi.org/10.7554/eLife.30244
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