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| <StructureSection load='6g70' size='340' side='right'caption='[[6g70]], [[Resolution|resolution]] 3.30Å' scene=''> | | <StructureSection load='6g70' size='340' side='right'caption='[[6g70]], [[Resolution|resolution]] 3.30Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[6g70]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6G70 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6G70 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6g70]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6G70 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6G70 FirstGlance]. <br> |
- | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Prpf39 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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]] 3.3Å</td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6g70 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6g70 OCA], [http://pdbe.org/6g70 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6g70 RCSB], [http://www.ebi.ac.uk/pdbsum/6g70 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6g70 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=6g70 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6g70 OCA], [https://pdbe.org/6g70 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6g70 RCSB], [https://www.ebi.ac.uk/pdbsum/6g70 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6g70 ProSAT]</span></td></tr> |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/PRP39_MOUSE PRP39_MOUSE] Involved in pre-mRNA splicing. |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| </StructureSection> | | </StructureSection> |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
- | [[Category: Bortoli, F D.De]] | + | [[Category: De Bortoli FD]] |
- | [[Category: Heyd, F]] | + | [[Category: Heyd F]] |
- | [[Category: Loll, B]] | + | [[Category: Loll B]] |
- | [[Category: Wahl, M]] | + | [[Category: Wahl M]] |
- | [[Category: Hat repeat protein]]
| + | |
- | [[Category: Splicing]]
| + | |
- | [[Category: U1snrnp]]
| + | |
| Structural highlights
Function
PRP39_MOUSE Involved in pre-mRNA splicing.
Publication Abstract from PubMed
In the yeast U1 snRNP the Prp39/Prp42 heterodimer is essential for early steps of spliceosome assembly. In metazoans no Prp42 ortholog exists, raising the question how the heterodimer is functionally substituted. Here we present the crystal structure of murine PRPF39, which forms a homodimer. Structure-guided point mutations disrupt dimer formation and inhibit splicing, manifesting the homodimer as functional unit. PRPF39 expression is controlled by NMD-inducing alternative splicing in mice and human, suggesting a role in adapting splicing efficiency to cell type specific requirements. A phylogenetic analysis reveals coevolution of shortened U1 snRNA and the absence of Prp42, which correlates with overall splicing complexity in different fungi. While current models correlate the diversity of spliceosomal proteins with splicing complexity, our study highlights a contrary case. We find that organisms with higher splicing complexity have substituted the Prp39/Prp42 heterodimer with a PRPF39 homodimer.
Increased versatility despite reduced molecular complexity: evolution, structure and function of metazoan splicing factor PRPF39.,De Bortoli F, Neumann A, Kotte A, Timmermann B, Schuler T, Wahl MC, Loll B, Heyd F Nucleic Acids Res. 2019 Apr 5. pii: 5428331. doi: 10.1093/nar/gkz243. PMID:30949712[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ De Bortoli F, Neumann A, Kotte A, Timmermann B, Schuler T, Wahl MC, Loll B, Heyd F. Increased versatility despite reduced molecular complexity: evolution, structure and function of metazoan splicing factor PRPF39. Nucleic Acids Res. 2019 Apr 5. pii: 5428331. doi: 10.1093/nar/gkz243. PMID:30949712 doi:http://dx.doi.org/10.1093/nar/gkz243
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