View source for 6ppp


==Structure of S. pombe Lsm2-8 with processed U6 snRNA==
<StructureSection load='6ppp' size='340' side='right'caption='[[6ppp]], [[Resolution|resolution]] 2.33&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.33&#8491;</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>
== Function ==
[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;">
== 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<ref>PMID:32518066</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6ppp" style="background-color:#fffaf0;"></div>

==See Also==
*[[Sm-like protein|Sm-like protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Schizosaccharomyces pombe 972h-]]
[[Category: Synthetic construct]]
[[Category: Butcher SE]]
[[Category: Montemayor EJ]]