2k3r

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==Pfu Rpp21 structure and assignments==
==Pfu Rpp21 structure and assignments==
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<StructureSection load='2k3r' size='340' side='right'caption='[[2k3r]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='2k3r' size='340' side='right'caption='[[2k3r]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2k3r]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43587 Atcc 43587]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K3R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K3R FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2k3r]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K3R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K3R FirstGlance]. <br>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rnp4, PF1613 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2261 ATCC 43587])</td></tr>
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<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>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ribonuclease_P Ribonuclease P], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.5 3.1.26.5] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2k3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k3r OCA], [https://pdbe.org/2k3r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k3r RCSB], [https://www.ebi.ac.uk/pdbsum/2k3r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k3r 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=2k3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k3r OCA], [https://pdbe.org/2k3r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k3r RCSB], [https://www.ebi.ac.uk/pdbsum/2k3r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k3r ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/RNP4_PYRFU RNP4_PYRFU]] Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. The RNA is catalytic, but its KM for pre-tRNA is 170-fold decreased in the presence of the 4 known protein subunits (Rnp1-4). The protein subunits also decrease the amount of Mg(2+) needed for activity.<ref>PMID:17053064</ref> <ref>PMID:21683084</ref> <ref>PMID:22298511</ref>
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[https://www.uniprot.org/uniprot/RNP4_PYRFU RNP4_PYRFU] Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. The RNA is catalytic, but its KM for pre-tRNA is 170-fold decreased in the presence of the 4 known protein subunits (Rnp1-4). The protein subunits also decrease the amount of Mg(2+) needed for activity.<ref>PMID:17053064</ref> <ref>PMID:21683084</ref> <ref>PMID:22298511</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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RNase P is the ubiquitous ribonucleoprotein metalloenzyme responsible for cleaving the 5'-leader sequence of precursor tRNAs during their maturation. While the RNA subunit is catalytically active on its own at high monovalent and divalent ion concentrations, four protein subunits are associated with archaeal RNase P activity in vivo: RPP21, RPP29, RPP30, and POP5. These proteins have been shown to function in pairs: RPP21-RPP29 and POP5-RPP30. We have determined the solution structure of RPP21 from the hyperthermophilic archaeon Pyrococcus furiosus ( Pfu) using conventional and paramagnetic NMR techniques. Pfu RPP21 in solution consists of an unstructured N-terminus, two alpha-helices, a zinc binding motif, and an unstructured C-terminus. Moreover, we have used chemical shift perturbations to characterize the interaction of RPP21 with RPP29. The data show that the primary contact with RPP29 is localized to the two helices of RPP21. This information represents a fundamental step toward understanding structure-function relationships of the archaeal RNase P holoenzyme.
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Solution structure of Pyrococcus furiosus RPP21, a component of the archaeal RNase P holoenzyme, and interactions with its RPP29 protein partner.,Amero CD, Boomershine WP, Xu Y, Foster M Biochemistry. 2008 Nov 11;47(45):11704-10. Epub 2008 Oct 16. PMID:18922021<ref>PMID:18922021</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2k3r" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 43587]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Ribonuclease P]]
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[[Category: Pyrococcus furiosus]]
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[[Category: Amero, C D]]
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[[Category: Amero CD]]
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[[Category: Boomershine, W P]]
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[[Category: Boomershine WP]]
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[[Category: Foster, M P]]
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[[Category: Foster MP]]
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[[Category: Xu, Y]]
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[[Category: Xu Y]]
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[[Category: Hydrolase]]
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[[Category: Pfu rpp21]]
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[[Category: Rnase p]]
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[[Category: Trna processing]]
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Current revision

Pfu Rpp21 structure and assignments

PDB ID 2k3r

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