3w3t: Difference between revisions
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<StructureSection load='3w3t' size='340' side='right'caption='[[3w3t]], [[Resolution|resolution]] 2.90Å' scene=''> | <StructureSection load='3w3t' size='340' side='right'caption='[[3w3t]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3w3t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3w3t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W3T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W3T FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</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=3w3t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w3t OCA], [https://pdbe.org/3w3t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w3t RCSB], [https://www.ebi.ac.uk/pdbsum/3w3t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w3t 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=3w3t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w3t OCA], [https://pdbe.org/3w3t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w3t RCSB], [https://www.ebi.ac.uk/pdbsum/3w3t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w3t ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/IMB3_YEAST IMB3_YEAST] Involved in the nuclear import of ribosomal proteins. Binds to nucleoporins and the GTP-bound form of GSP1 (Ran). Plays a role in protein secretion. | |||
<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: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Saccharomyces cerevisiae S288C]] | ||
[[Category: | [[Category: Kobayashi J]] | ||
[[Category: | [[Category: Matsuura Y]] | ||
Latest revision as of 15:48, 8 November 2023
Crystal structure of Kap121pCrystal structure of Kap121p
Structural highlights
FunctionIMB3_YEAST Involved in the nuclear import of ribosomal proteins. Binds to nucleoporins and the GTP-bound form of GSP1 (Ran). Plays a role in protein secretion. Publication Abstract from PubMedKap121p (also known as Pse1p) is an essential karyopherin that mediates nuclear import of a plethora of cargoes including cell-cycle regulators, transcription factors, and ribosomal proteins in Saccharomyces cerevisiae. It has been proposed that the spindle assembly checkpoint signaling triggers molecular rearrangements of nuclear pore complexes and thereby arrests Kap121p-mediated nuclear import at metaphase, while leaving import mediated by other karyopherins unaffected. The Kap121p-specific import inhibition is required for normal progression through mitosis. To understand the structural basis for Kap121p-mediated nuclear import and its unique regulatory mechanism during mitosis, we determined crystal structures of Kap121p in isolation and also in complex with either its import cargoes or nucleoporin Nup53p or RanGTP. Kap121p has a superhelical structure composed of 24 HEAT repeats. The structures of Kap121p-cargo complexes define a non-conventional nuclear localization signal (NLS) that has a consensus sequence of KV/IxKx1-2K/H/R. The structure of Kap121p-Nup53p complex shows that cargo and Nup53p compete for the same high-affinity binding site, explaining how Nup53p binding forces cargo release when the Kap121p binding site of Nup53p is exposed during mitosis. Comparison of the NLS- and RanGTP-complexes reveals that RanGTP binding not only occludes the cargo-binding site but also forces Kap121p into a conformation that is incompatible with NLS recognition. Structural basis for cell-cycle dependent nuclear import mediated by the karyopherin Kap121p.,Kobayashi J, Matsuura Y J Mol Biol. 2013 Mar 27. pii: S0022-2836(13)00194-0. doi:, 10.1016/j.jmb.2013.02.035. PMID:23541588[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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