5ft9: Difference between revisions

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<StructureSection load='5ft9' size='340' side='right'caption='[[5ft9]], [[Resolution|resolution]] 3.05&Aring;' scene=''>
<StructureSection load='5ft9' size='340' side='right'caption='[[5ft9]], [[Resolution|resolution]] 3.05&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<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>
<table><tr><td colspan='2'>[[5ft9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. 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 [https://proteopedia.org/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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.05&#8491;</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://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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ft9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ft9 OCA], [https://pdbe.org/5ft9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ft9 RCSB], [https://www.ebi.ac.uk/pdbsum/5ft9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ft9 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/PRRP2_ARATH 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).<ref>PMID:22549728</ref> 
[https://www.uniprot.org/uniprot/PRRP2_ARATH 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).<ref>PMID:22549728</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
RNase 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<ref>PMID:26527263</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5ft9" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Ribonuclease|Ribonuclease]]
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Arath]]
[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Ribonuclease P]]
[[Category: Fernandez-Millan P]]
[[Category: Fernandez-Millan, P]]
[[Category: Giege P]]
[[Category: Giege, P]]
[[Category: Gobert A]]
[[Category: Gobert, A]]
[[Category: Pinker F]]
[[Category: Pinker, F]]
[[Category: Sauter C]]
[[Category: Sauter, C]]
[[Category: Schelcher C]]
[[Category: Schelcher, C]]
[[Category: Hydrolase]]
[[Category: Ppr]]
[[Category: Prorp]]
[[Category: Proteinaceous rnase p]]
[[Category: Trna 5' maturation]]

Latest revision as of 13:23, 26 July 2023

Arabidopsis thaliana nuclear protein-only RNase P 2 (PRORP2)

5ft9, resolution 3.05Å

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