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| ==Crystal structure of human RPP40== | | ==Crystal structure of human RPP40== |
| <StructureSection load='6ahv' size='340' side='right' caption='[[6ahv]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='6ahv' size='340' side='right'caption='[[6ahv]], [[Resolution|resolution]] 2.60Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[6ahv]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AHV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AHV FirstGlance]. <br> | | <table><tr><td colspan='2'>[[6ahv]] is a 1 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=6AHV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6AHV FirstGlance]. <br> |
| </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6ahr|6ahr]]</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]] 2.6Å</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6ahv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ahv OCA], [https://pdbe.org/6ahv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ahv RCSB], [https://www.ebi.ac.uk/pdbsum/6ahv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ahv ProSAT]</span></td></tr> |
| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ahv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ahv OCA], [http://pdbe.org/6ahv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ahv RCSB], [http://www.ebi.ac.uk/pdbsum/6ahv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ahv ProSAT]</span></td></tr> | |
| </table> | | </table> |
| == Function == | | == Function == |
| [[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. | | [https://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. |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| 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>
| | ==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 6ahv" style="background-color:#fffaf0;"></div>
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| == References == | |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Ribonuclease P]] | | [[Category: Homo sapiens]] |
| [[Category: Lan, P]] | | [[Category: Large Structures]] |
| [[Category: Lei, M]] | | [[Category: Lan P]] |
| [[Category: Niu, S]] | | [[Category: Lei M]] |
| [[Category: Tan, M]] | | [[Category: Niu S]] |
| [[Category: Wu, J]] | | [[Category: Tan M]] |
| [[Category: Hydrolase]]
| | [[Category: Wu J]] |
| [[Category: Rnase p]]
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