2my2
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Snu17p-Bud13p structure intermediate during RES complex assembly== | |
| + | <StructureSection load='2my2' size='340' side='right'caption='[[2my2]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2my2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MY2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MY2 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2my2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2my2 OCA], [https://pdbe.org/2my2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2my2 RCSB], [https://www.ebi.ac.uk/pdbsum/2my2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2my2 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/IST3_YEAST IST3_YEAST] Required for pre-mRNA splicing and spliceosome assembly. As part of the pre-mRNA retention and splicing (RES) complex, required for nuclear pre-mRNA retention and efficient splicing. Required for MER1-activated splicing.<ref>PMID:11287609</ref> <ref>PMID:15565172</ref> <ref>PMID:14973223</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The action of the spliceosome depends on the stepwise cooperative assembly and disassembly of its components. Very strong cooperativity was observed for the RES (Retention and Splicing) hetero-trimeric complex where the affinity from binary to tertiary interactions changes more than 100-fold and affects RNA binding. The RES complex is involved in splicing regulation and retention of not properly spliced pre-mRNA with its three components-Snu17p, Pml1p and Bud13p-giving rise to the two possible intermediate dimeric complexes Pml1p-Snu17p and Bud13p-Snu17p. Here we determined the three-dimensional structure and dynamics of the Pml1p-Snu17p and Bud13p-Snu17p dimers using liquid state NMR. We demonstrate that localized as well as global changes occur along the RES trimer assembly pathway. The stepwise rigidification of the Snu17p structure following the binding of Pml1p and Bud13p provides a basis for the strong cooperative nature of RES complex assembly. | ||
| - | + | Structures of intermediates during RES complex assembly.,Wysoczanski P, Becker S, Zweckstetter M Sci Rep. 2015 Jul 27;5:12545. doi: 10.1038/srep12545. PMID:26212312<ref>PMID:26212312</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 2my2" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | |
| - | [[Category: Wysoczanski | + | ==See Also== |
| + | *[[Increased sodium tolerance protein|Increased sodium tolerance protein]] | ||
| + | *[[Pre-mRNA splicing factors 3D structures|Pre-mRNA splicing factors 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Saccharomyces cerevisiae S288C]] | ||
| + | [[Category: Becker S]] | ||
| + | [[Category: Wysoczanski P]] | ||
| + | [[Category: Zweckstetter M]] | ||
Current revision
Snu17p-Bud13p structure intermediate during RES complex assembly
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