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6ahr

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Revision as of 23:05, 10 April 2020

Cryo-EM structure of human Ribonuclease P

6ahr, resolution 3.92Å

Structural highlights

6ahr is a 12 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Activity:	Ribonuclease P, with EC number 3.1.26.5
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[POP1_HUMAN] Anauxetic dysplasia. The disease is caused by mutations affecting the gene represented in this entry.

Function

[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. [RPP40_HUMAN] Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. [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. [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. [RPP30_HUMAN] Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. [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. [RPP14_HUMAN] Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. [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. [RPP21_HUMAN] Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. [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.^[1]

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.

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ van Eenennaam H, Lugtenberg D, Vogelzangs JH, van Venrooij WJ, Pruijn GJ. hPop5, a protein subunit of the human RNase MRP and RNase P endoribonucleases. J Biol Chem. 2001 Aug 24;276(34):31635-41. doi: 10.1074/jbc.M103399200. Epub 2001, Jun 18. PMID:11413139 doi:http://dx.doi.org/10.1074/jbc.M103399200
↑ Wu J, Niu S, Tan M, Huang C, Li M, Song Y, Wang Q, Chen J, Shi S, Lan P, Lei M. Cryo-EM Structure of the Human Ribonuclease P Holoenzyme. Cell. 2018 Nov 15;175(5):1393-1404.e11. doi: 10.1016/j.cell.2018.10.003. Epub, 2018 Oct 25. PMID:30454648 doi:http://dx.doi.org/10.1016/j.cell.2018.10.003

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6ahr"

@@ Line 3: / Line 3: @@
 <SX load='6ahr' size='340' side='right' viewer='molstar' caption='[[6ahr]], [[Resolution|resolution]] 3.92&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6ahr]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AHR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AHR FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6ahr]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AHR OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6AHR FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</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='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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ahr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ahr OCA], [http://pdbe.org/6ahr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ahr RCSB], [http://www.ebi.ac.uk/pdbsum/6ahr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ahr ProSAT]</span></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=6ahr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ahr OCA], [http://pdbe.org/6ahr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ahr RCSB], [http://www.ebi.ac.uk/pdbsum/6ahr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ahr ProSAT]</span></td></tr>
 </table>
 == Disease ==

6ahr

From Proteopedia

Revision as of 23:05, 10 April 2020

Cryo-EM structure of human Ribonuclease P

Structural highlights

Disease

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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