|
|
| Line 3: |
Line 3: |
| | <StructureSection load='6ppp' size='340' side='right'caption='[[6ppp]], [[Resolution|resolution]] 2.33Å' scene=''> | | <StructureSection load='6ppp' size='340' side='right'caption='[[6ppp]], [[Resolution|resolution]] 2.33Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6ppp]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Fission_yeast Fission yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PPP OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6PPP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6ppp]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe_972h- Schizosaccharomyces pombe 972h-] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PPP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PPP FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lsm2, SPCC1620.01c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284812 Fission yeast]), lsm3, SPBC9B6.05c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284812 Fission yeast]), lsm4, SPBC30D10.06 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284812 Fission yeast]), lsm5, SPBC20F10.09 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284812 Fission yeast]), lsm6, SPAC2F3.17c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284812 Fission yeast]), lsm7, SPCC285.12 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284812 Fission yeast]), lsm8, SPCC1840.10 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284812 Fission yeast])</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]] 2.33Å</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=6ppp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ppp OCA], [http://pdbe.org/6ppp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ppp RCSB], [http://www.ebi.ac.uk/pdbsum/6ppp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ppp 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=6ppp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ppp OCA], [https://pdbe.org/6ppp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ppp RCSB], [https://www.ebi.ac.uk/pdbsum/6ppp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ppp ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/LSM6_SCHPO LSM6_SCHPO]] Component of LSm protein complexes, which are involved in RNA processing and may function in a chaperone-like manner, facilitating the efficient association of RNA processing factors with their substrates. Component of the cytoplasmic LSM1-LSM7 complex, which is thought to be involved in mRNA degradation by activating the decapping step in the 5'-to-3' mRNA decay pathway. Component of the nuclear LSM2-LSM8 complex, which is involved in splicing of nuclear mRNAs. LSM2-LSM8 associates with multiple snRNP complexes containing the U6 snRNA (U4/U6 di-snRNP, spliceosomal U4/U6.U5 tri-snRNP, and free U6 snRNP). It binds directly to the 3'-terminal U-tract of U6 snRNA and plays a role in the biogenesis and stability of the U6 snRNP and U4/U6 snRNP complexes. LSM2-LSM8 probably also is involved degradation of nuclear pre-mRNA by targeting them for decapping, and in processing of pre-tRNAs, pre-rRNAs and U3 snoRNA (By similarity). [[http://www.uniprot.org/uniprot/LSM3_SCHPO LSM3_SCHPO]] Binds specifically to the 3'-terminal U-tract of U6 snRNA. [[http://www.uniprot.org/uniprot/LSM7_SCHPO LSM7_SCHPO]] Component of LSm protein complexes, which are involved in RNA processing and may function in a chaperone-like manner. Probable component of the spliceosome. [[http://www.uniprot.org/uniprot/LSM2_SCHPO LSM2_SCHPO]] Binds specifically to the 3'-terminal U-tract of U6 snRNA. [[http://www.uniprot.org/uniprot/LSM8_SCHPO LSM8_SCHPO]] Probable component of the spliceosome. [[http://www.uniprot.org/uniprot/LSM4_SCHPO LSM4_SCHPO]] Binds specifically to the 3'-terminal U-tract of U6 snRNA. [[http://www.uniprot.org/uniprot/LSM5_SCHPO LSM5_SCHPO]] Component of LSm protein complexes, which are involved in RNA processing and may function in a chaperone-like manner. LSm5 is required for processing of pre-tRNAs, pre-rRNAs and U3 snoRNA (By similarity). | + | [https://www.uniprot.org/uniprot/LSM2_SCHPO LSM2_SCHPO] Binds specifically to the 3'-terminal U-tract of U6 snRNA. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 18: |
Line 18: |
| | </div> | | </div> |
| | <div class="pdbe-citations 6ppp" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6ppp" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Sm-like protein|Sm-like protein]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Fission yeast]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Butcher, S E]] | + | [[Category: Schizosaccharomyces pombe 972h-]] |
| - | [[Category: Montemayor, E J]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Rna]] | + | [[Category: Butcher SE]] |
| - | [[Category: Rna binding protein]] | + | [[Category: Montemayor EJ]] |
| - | [[Category: Rna binding protein-rna complex]]
| + | |
| Structural highlights
Function
LSM2_SCHPO Binds specifically to the 3'-terminal U-tract of U6 snRNA.
Publication Abstract from PubMed
Eukaryotes possess eight highly conserved Lsm (like Sm) proteins that assemble into circular, heteroheptameric complexes, bind RNA, and direct a diverse range of biological processes. Among the many essential functions of Lsm proteins, the cytoplasmic Lsm1-7 complex initiates mRNA decay, while the nuclear Lsm2-8 complex acts as a chaperone for U6 spliceosomal RNA. It has been unclear how these complexes perform their distinct functions while differing by only one out of seven subunits. Here, we elucidate the molecular basis for Lsm-RNA recognition and present four high-resolution structures of Lsm complexes bound to RNAs. The structures of Lsm2-8 bound to RNA identify the unique 2',3' cyclic phosphate end of U6 as a prime determinant of specificity. In contrast, the Lsm1-7 complex strongly discriminates against cyclic phosphates and tightly binds to oligouridylate tracts with terminal purines. Lsm5 uniquely recognizes purine bases, explaining its divergent sequence relative to other Lsm subunits. Lsm1-7 loads onto RNA from the 3' end and removal of the Lsm1 C-terminal region allows Lsm1-7 to scan along RNA, suggesting a gated mechanism for accessing internal binding sites. These data reveal the molecular basis for RNA binding by Lsm proteins, a fundamental step in the formation of molecular assemblies that are central to eukaryotic mRNA metabolism.
Molecular basis for the distinct cellular functions of the Lsm1-7 and Lsm2-8 complexes.,Montemayor EJ, Virta JM, Hayes SM, Nomura Y, Brow DA, Butcher SE RNA. 2020 Jun 9. pii: rna.075879.120. doi: 10.1261/rna.075879.120. PMID:32518066[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Montemayor EJ, Virta JM, Hayes SM, Nomura Y, Brow DA, Butcher SE. Molecular basis for the distinct cellular functions of the Lsm1-7 and Lsm2-8 complexes. RNA. 2020 Jun 9. pii: rna.075879.120. doi: 10.1261/rna.075879.120. PMID:32518066 doi:http://dx.doi.org/10.1261/rna.075879.120
|
