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| | <StructureSection load='6nqi' size='340' side='right'caption='[[6nqi]], [[Resolution|resolution]] 2.75Å' scene=''> | | <StructureSection load='6nqi' size='340' side='right'caption='[[6nqi]], [[Resolution|resolution]] 2.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6nqi]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cyam1 Cyam1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NQI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NQI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6nqi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cyanidioschyzon_merolae_strain_10D Cyanidioschyzon merolae strain 10D]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NQI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6NQI FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</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]] 2.75Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CYME_CMH168C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=280699 CYAM1])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</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=6nqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nqi OCA], [http://pdbe.org/6nqi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6nqi RCSB], [http://www.ebi.ac.uk/pdbsum/6nqi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6nqi 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=6nqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nqi OCA], [https://pdbe.org/6nqi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6nqi RCSB], [https://www.ebi.ac.uk/pdbsum/6nqi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6nqi ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/M1V7K2_CYAM1 M1V7K2_CYAM1] |
| | <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: Cyam1]] | + | [[Category: Cyanidioschyzon merolae strain 10D]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Garside, E L]] | + | [[Category: Garside EL]] |
| - | [[Category: MacMillan, A M]] | + | [[Category: MacMillan AM]] |
| - | [[Category: Rnase h]]
| + | |
| - | [[Category: Spliceosome]]
| + | |
| - | [[Category: Splicing]]
| + | |
| Structural highlights
Function
M1V7K2_CYAM1
Publication Abstract from PubMed
Conformational rearrangements are critical to regulating the assembly and activity of the spliceosome. The spliceosomal protein Prp8 undergoes multiple conformational changes during the course of spliceosome assembly, activation, and catalytic activity. Most of these rearrangements of Prp8 involve the disposition of the C-terminal Jab-MPN and RH domains with respect to the core of Prp8. Here we use X-ray structural analysis to show that a previously characterized and highly conserved beta-hairpin structure in the RH domain, that acts as a toggle in the spliceosome, is absent in Prp8 from the reduced spliceosome of the red alga C. merolae. Using comparative sequence analysis, we show that the presence or absence of this hairpin corresponds to the presence or absence of protein partners that interact with this hairpin as observed by X-ray and cryo-EM studies. The presence of the toggle correlates with increasing intron number suggesting a role in the regulation of splicing.
Prp8 in a Reduced Spliceosome Lacks a Conserved Toggle that Correlates with Splicing Complexity across Diverse Taxa.,Garside EL, Whelan TA, Stark MR, Rader SD, Fast NM, MacMillan AM J Mol Biol. 2019 May 9. pii: S0022-2836(19)30257-8. doi:, 10.1016/j.jmb.2019.04.047. PMID:31078556[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Garside EL, Whelan TA, Stark MR, Rader SD, Fast NM, MacMillan AM. Prp8 in a Reduced Spliceosome Lacks a Conserved Toggle that Correlates with Splicing Complexity across Diverse Taxa. J Mol Biol. 2019 May 9. pii: S0022-2836(19)30257-8. doi:, 10.1016/j.jmb.2019.04.047. PMID:31078556 doi:http://dx.doi.org/10.1016/j.jmb.2019.04.047
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