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| <StructureSection load='7c79' size='340' side='right'caption='[[7c79]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='7c79' size='340' side='right'caption='[[7c79]], [[Resolution|resolution]] 2.50Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[7c79]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast] and [http://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=7C79 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7C79 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[7c79]] is a 11 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=7C79 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7C79 FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.5Å</td></tr> |
| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribonuclease_P Ribonuclease P], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.5 3.1.26.5] </span></td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=7c79 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7c79 OCA], [http://pdbe.org/7c79 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7c79 RCSB], [http://www.ebi.ac.uk/pdbsum/7c79 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7c79 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=7c79 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7c79 OCA], [https://pdbe.org/7c79 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7c79 RCSB], [https://www.ebi.ac.uk/pdbsum/7c79 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7c79 ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/POP6_YEAST POP6_YEAST]] Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP, which cleaves pre-rRNA sequences.<ref>PMID:9620854</ref> [[http://www.uniprot.org/uniprot/RMP1_YEAST RMP1_YEAST]] Functions as part of ribonuclease MRP (RNase MRP), which is involved in rRNA processing in mitochondria.<ref>PMID:15637077</ref> [[http://www.uniprot.org/uniprot/POP3_YEAST POP3_YEAST]] Required for processing of 5.8S rRNA (short form) at site A3 and for 5'- and 3'-processing of pre-tRNA.<ref>PMID:9029160</ref> <ref>PMID:9620854</ref> [[http://www.uniprot.org/uniprot/POP7_YEAST POP7_YEAST]] Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP, which cleaves pre-rRNA sequences.<ref>PMID:9618478</ref> <ref>PMID:9620854</ref> [[http://www.uniprot.org/uniprot/RPP1_YEAST RPP1_YEAST]] Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP, which cleaves pre-rRNA sequences.<ref>PMID:9308968</ref> <ref>PMID:9620854</ref> [[http://www.uniprot.org/uniprot/POP1_YEAST POP1_YEAST]] Required for processing of 5.8S rRNA (short form) at site A3 and for 5' and 3' processing of pre-tRNA.<ref>PMID:7926742</ref> <ref>PMID:9620854</ref> [[http://www.uniprot.org/uniprot/POP8_YEAST POP8_YEAST]] Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP, which cleaves pre-rRNA sequences.<ref>PMID:9620854</ref> [[http://www.uniprot.org/uniprot/POP4_YEAST POP4_YEAST]] Required for 5.8S rRNA and tRNA processing; associated with RNase MRP and RNase P.<ref>PMID:9085845</ref> <ref>PMID:9620854</ref> [[http://www.uniprot.org/uniprot/RMRP_YEAST RMRP_YEAST]] Essential component of the MRP ribonucleoprotein endoribonuclease that cleaves mitochondrial primer RNA sequences.<ref>PMID:7958920</ref> [[http://www.uniprot.org/uniprot/POP5_YEAST POP5_YEAST]] Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP, which cleaves pre-rRNA sequences.<ref>PMID:9620854</ref> | | [https://www.uniprot.org/uniprot/POP1_YEAST POP1_YEAST] Required for processing of 5.8S rRNA (short form) at site A3 and for 5' and 3' processing of pre-tRNA.<ref>PMID:7926742</ref> <ref>PMID:9620854</ref> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Ribonuclease (RNase) MRP is a conserved eukaryotic ribonucleoprotein complex that plays essential roles in pre-ribosomal RNA (pre-rRNA) processing and cell cycle regulation. In contrast to RNase P, which selectively cleaves tRNA-like substrates, it has remained a mystery how RNase MRP recognizes its diverse substrates. To address this question, we determined cryo-EM structures of Saccharomyces cerevisiae RNase MRP alone and in complex with a fragment of pre-rRNA. These structures combined with biochemical studies reveal that co-evolution of both protein and RNA subunits has transformed RNase MRP into a distinct ribonuclease that processes single-stranded RNAs by recognizing a short, loosely-defined consensus sequence. This broad substrate specificity suggests that RNase MRP may have myriad yet unrecognized substrates that could play important roles in various cellular contexts.
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| Structural insight into precursor ribosomal RNA processing by ribonuclease MRP.,Lan P, Zhou B, Tan M, Li S, Cao M, Wu J, Lei M Science. 2020 Jun 25. pii: science.abc0149. doi: 10.1126/science.abc0149. PMID:32586950<ref>PMID:32586950</ref>
| | ==See Also== |
| | | *[[Ribonuclease 3D structures|Ribonuclease 3D structures]] |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 7c79" style="background-color:#fffaf0;"></div>
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| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Baker's yeast]]
| |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Ribonuclease P]]
| | [[Category: Saccharomyces cerevisiae S288C]] |
| [[Category: Saccharomyces cerevisiae s288c]] | | [[Category: Lan P]] |
| [[Category: Lan, P]] | | [[Category: Lei M]] |
| [[Category: Lei, M]] | | [[Category: Wu J]] |
| [[Category: Wu, J]] | |
| [[Category: Ribonuclease mrp]]
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| [[Category: Rna binding protein]]
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| [[Category: Rna-protein complex]]
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