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| <SX load='6ahu' size='340' side='right' viewer='molstar' caption='[[6ahu]], [[Resolution|resolution]] 3.66Å' scene=''> | | <SX load='6ahu' size='340' side='right' viewer='molstar' caption='[[6ahu]], [[Resolution|resolution]] 3.66Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[6ahu]] is a 13 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AHU OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6AHU FirstGlance]. <br> | | <table><tr><td colspan='2'>[[6ahu]] is a 11 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AHU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6AHU FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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]] 3.66Å</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=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=6ahu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ahu OCA], [http://pdbe.org/6ahu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ahu RCSB], [http://www.ebi.ac.uk/pdbsum/6ahu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ahu 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=6ahu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ahu OCA], [https://pdbe.org/6ahu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ahu RCSB], [https://www.ebi.ac.uk/pdbsum/6ahu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ahu ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Disease == | | == Disease == |
| [[http://www.uniprot.org/uniprot/POP1_HUMAN POP1_HUMAN]] Anauxetic dysplasia. The disease is caused by mutations affecting the gene represented in this entry. | | [https://www.uniprot.org/uniprot/POP1_HUMAN POP1_HUMAN] Anauxetic dysplasia. The disease is caused by mutations affecting the gene represented in this entry. |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/RPP25_HUMAN RPP25_HUMAN]] Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP. This subunit binds to RNA. [[http://www.uniprot.org/uniprot/RPP40_HUMAN RPP40_HUMAN]] Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. [[http://www.uniprot.org/uniprot/RPP38_HUMAN RPP38_HUMAN]] Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. RPP38 may associate transiently with RNase P RNA as a factor involved in the transport of H1 RNA to the putative site of its assembly in the cell, the nucleolus. [[http://www.uniprot.org/uniprot/POP7_HUMAN POP7_HUMAN]] Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP complex, which cleaves pre-rRNA sequences. [[http://www.uniprot.org/uniprot/RPP30_HUMAN RPP30_HUMAN]] Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. [[http://www.uniprot.org/uniprot/POP1_HUMAN POP1_HUMAN]] Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP. [[http://www.uniprot.org/uniprot/RPP14_HUMAN RPP14_HUMAN]] Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. [[http://www.uniprot.org/uniprot/RPP29_HUMAN RPP29_HUMAN]] Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. May function with RPP38 to coordinate the nucleolar targeting and/or assembly of RNase P. [[http://www.uniprot.org/uniprot/RPP21_HUMAN RPP21_HUMAN]] Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. [[http://www.uniprot.org/uniprot/POP5_HUMAN POP5_HUMAN]] Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP.<ref>PMID:11413139</ref> | | [https://www.uniprot.org/uniprot/POP1_HUMAN POP1_HUMAN] Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP. |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
| |
| Ribonuclease (RNase) P is a ubiquitous ribozyme that cleaves the 5' leader from precursor tRNAs. Here, we report cryo-electron microscopy structures of the human nuclear RNase P alone and in complex with tRNA(Val). Human RNase P is a large ribonucleoprotein complex that contains 10 protein components and one catalytic RNA. The protein components form an interlocked clamp that stabilizes the RNA in a conformation optimal for substrate binding. Human RNase P recognizes the tRNA using a double-anchor mechanism through both protein-RNA and RNA-RNA interactions. Structural comparison of the apo and tRNA-bound human RNase P reveals that binding of tRNA induces a local conformational change in the catalytic center, transforming the ribozyme into an active state. Our results also provide an evolutionary model depicting how auxiliary RNA elements in bacterial RNase P, essential for substrate binding, and catalysis, were replaced by the much more complex and multifunctional protein components in higher organisms.
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| Cryo-EM Structure of the Human Ribonuclease P Holoenzyme.,Wu J, Niu S, Tan M, Huang C, Li M, Song Y, Wang Q, Chen J, Shi S, Lan P, Lei M Cell. 2018 Nov 15;175(5):1393-1404.e11. doi: 10.1016/j.cell.2018.10.003. Epub, 2018 Oct 25. PMID:30454648<ref>PMID:30454648</ref>
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| 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 6ahu" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[Ribonuclease 3D structures|Ribonuclease 3D structures]] | | *[[Ribonuclease 3D structures|Ribonuclease 3D structures]] |
| == References ==
| |
| <references/>
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| __TOC__ | | __TOC__ |
| </SX> | | </SX> |
| [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Ribonuclease P]]
| | [[Category: Lan P]] |
| [[Category: Lan, P]] | | [[Category: Lei M]] |
| [[Category: Lei, M]] | | [[Category: Niu S]] |
| [[Category: Niu, S]] | | [[Category: Tan M]] |
| [[Category: Tan, M]] | | [[Category: Wu J]] |
| [[Category: Wu, J]] | |
| [[Category: Hydrolase-rna complex]]
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| [[Category: Ribonuclease p]]
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| [[Category: Rna-protein complex]]
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