5ft9: Difference between revisions
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==Arabidopsis thaliana nuclear protein-only RNase P 2 (PRORP2)== | ==Arabidopsis thaliana nuclear protein-only RNase P 2 (PRORP2)== | ||
<StructureSection load='5ft9' size='340' side='right' caption='[[5ft9]], [[Resolution|resolution]] 3.05Å' scene=''> | <StructureSection load='5ft9' size='340' side='right' caption='[[5ft9]], [[Resolution|resolution]] 3.05Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5ft9]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FT9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FT9 FirstGlance]. <br> | <table><tr><td colspan='2'>[[5ft9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FT9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FT9 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"><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='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=5ft9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ft9 OCA], [http://pdbe.org/5ft9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ft9 RCSB], [http://www.ebi.ac.uk/pdbsum/5ft9 PDBsum]</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=5ft9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ft9 OCA], [http://pdbe.org/5ft9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ft9 RCSB], [http://www.ebi.ac.uk/pdbsum/5ft9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ft9 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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</div> | </div> | ||
<div class="pdbe-citations 5ft9" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5ft9" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Ribonuclease|Ribonuclease]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Arath]] | |||
[[Category: Ribonuclease P]] | [[Category: Ribonuclease P]] | ||
[[Category: Fernandez-Millan, P]] | [[Category: Fernandez-Millan, P]] | ||
Revision as of 11:15, 6 March 2019
Arabidopsis thaliana nuclear protein-only RNase P 2 (PRORP2)Arabidopsis thaliana nuclear protein-only RNase P 2 (PRORP2)
Structural highlights
Function[PRRP2_ARATH] Endonuclease RNase P responsible for the 5' maturation of tRNA precursors. Also involved in the maturation of mRNA and small nucleolar RNA (snoRNA).[1] Publication Abstract from PubMedRNase P activity is ubiquitous and involves the 5' maturation of precursor tRNAs. For a long time, it was thought that all RNases P were ribonucleoproteic enzymes. However, the characterization of RNase P in human mitochondria and in plants revealed a novel kind of RNase P composed of protein only, called PRORP for `proteinaceous RNase P'. Whereas in human mitochondria PRORP has two partners that are required for RNase P activity, PRORP proteins are active as single-subunit enzymes in plants. Three paralogues of PRORP are found in Arabidopsis thaliana. PRORP1 is responsible for RNase P in mitochondria and chloroplasts, while PRORP2 and PRORP3 are nuclear enzymes. Here, the purification and crystallization of the Arabidopsis PRORP2 protein are reported. Optimization of the initial crystallization conditions led to crystals that diffracted to 3 A resolution. Crystallization and crystallographic analysis of an Arabidopsis nuclear proteinaceous RNase P.,Pinker F, Giege P, Sauter C Acta Crystallogr F Struct Biol Commun. 2015 Nov 1;71(Pt 11):1372-7. doi:, 10.1107/S2053230X15017033. Epub 2015 Oct 23. PMID:26527263[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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