4m75: Difference between revisions
New page: '''Unreleased structure''' The entry 4m75 is ON HOLD Authors: Zhou, L., Hang, J., Zhou, Y., Wan, R., Lu, G., Yan, C., Shi, Y. Description: Crystal structure of protein complex |
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The | ==Crystal structure of Lsm1-7 complex== | ||
<StructureSection load='4m75' size='340' side='right'caption='[[4m75]], [[Resolution|resolution]] 2.95Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4m75]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M75 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4M75 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]] 2.95Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=4m75 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m75 OCA], [https://pdbe.org/4m75 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4m75 RCSB], [https://www.ebi.ac.uk/pdbsum/4m75 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4m75 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/LSM1_YEAST LSM1_YEAST] Component of the cytoplasmic LSM1-LSM7 complex which is involved in mRNA degradation by activating the decapping step.<ref>PMID:10747033</ref> <ref>PMID:10913177</ref> <ref>PMID:10761922</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Splicing of precursor messenger RNA (pre-mRNA) in eukaryotic cells is carried out by the spliceosome, which consists of five small nuclear ribonucleoproteins (snRNPs) and a number of accessory factors and enzymes. Each snRNP contains a ring-shaped subcomplex of seven proteins and a specific RNA molecule. The U6 snRNP contains a unique heptameric Lsm protein complex, which specifically recognizes the U6 small nuclear RNA at its 3' end. Here we report the crystal structures of the heptameric Lsm complex, both by itself and in complex with a 3' fragment of U6 snRNA, at 2.8 A resolution. Each of the seven Lsm proteins interacts with two neighbouring Lsm components to form a doughnut-shaped assembly, with the order Lsm3-2-8-4-7-5-6. The four uridine nucleotides at the 3' end of U6 snRNA are modularly recognized by Lsm3, Lsm2, Lsm8 and Lsm4, with the uracil base specificity conferred by a highly conserved asparagine residue. The uracil base at the extreme 3' end is sandwiched by His 36 and Arg 69 from Lsm3, through pi-pi and cation-pi interactions, respectively. The distinctive end-recognition of U6 snRNA by the Lsm complex contrasts with RNA binding by the Sm complex in the other snRNPs. The structural features and associated biochemical analyses deepen mechanistic understanding of the U6 snRNP function in pre-mRNA splicing. | |||
Crystal structures of the Lsm complex bound to the 3' end sequence of U6 small nuclear RNA.,Zhou L, Hang J, Zhou Y, Wan R, Lu G, Yin P, Yan C, Shi Y Nature. 2013 Nov 17. doi: 10.1038/nature12803. PMID:24240276<ref>PMID:24240276</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4m75" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Sm-like protein 3D structures|Sm-like protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Saccharomyces cerevisiae S288C]] | |||
[[Category: Hang J]] | |||
[[Category: Lu G]] | |||
[[Category: Shi Y]] | |||
[[Category: Wan R]] | |||
[[Category: Yan C]] | |||
[[Category: Zhou L]] | |||
[[Category: Zhou Y]] | |||
Latest revision as of 11:27, 6 December 2023
Crystal structure of Lsm1-7 complexCrystal structure of Lsm1-7 complex
Structural highlights
FunctionLSM1_YEAST Component of the cytoplasmic LSM1-LSM7 complex which is involved in mRNA degradation by activating the decapping step.[1] [2] [3] Publication Abstract from PubMedSplicing of precursor messenger RNA (pre-mRNA) in eukaryotic cells is carried out by the spliceosome, which consists of five small nuclear ribonucleoproteins (snRNPs) and a number of accessory factors and enzymes. Each snRNP contains a ring-shaped subcomplex of seven proteins and a specific RNA molecule. The U6 snRNP contains a unique heptameric Lsm protein complex, which specifically recognizes the U6 small nuclear RNA at its 3' end. Here we report the crystal structures of the heptameric Lsm complex, both by itself and in complex with a 3' fragment of U6 snRNA, at 2.8 A resolution. Each of the seven Lsm proteins interacts with two neighbouring Lsm components to form a doughnut-shaped assembly, with the order Lsm3-2-8-4-7-5-6. The four uridine nucleotides at the 3' end of U6 snRNA are modularly recognized by Lsm3, Lsm2, Lsm8 and Lsm4, with the uracil base specificity conferred by a highly conserved asparagine residue. The uracil base at the extreme 3' end is sandwiched by His 36 and Arg 69 from Lsm3, through pi-pi and cation-pi interactions, respectively. The distinctive end-recognition of U6 snRNA by the Lsm complex contrasts with RNA binding by the Sm complex in the other snRNPs. The structural features and associated biochemical analyses deepen mechanistic understanding of the U6 snRNP function in pre-mRNA splicing. Crystal structures of the Lsm complex bound to the 3' end sequence of U6 small nuclear RNA.,Zhou L, Hang J, Zhou Y, Wan R, Lu G, Yin P, Yan C, Shi Y Nature. 2013 Nov 17. doi: 10.1038/nature12803. PMID:24240276[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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