4xgm: Difference between revisions

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 ==Structure of the nuclease subunit of human mitochondrial RNase P (MRPP3) at 1.98A==
-<StructureSection load='4xgm' size='340' side='right' caption='[[4xgm]], [[Resolution|resolution]] 1.98&Aring;' scene=''>
+<StructureSection load='4xgm' size='340' side='right'caption='[[4xgm]], [[Resolution|resolution]] 1.98&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4xgm]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XGM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XGM FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4xgm]] 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=4XGM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XGM FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <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]] 1.98&#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=GOL:GLYCEROL'>GOL</scene>, <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=4xgm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xgm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4xgm RCSB], [http://www.ebi.ac.uk/pdbsum/4xgm PDBsum]</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=4xgm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xgm OCA], [https://pdbe.org/4xgm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xgm RCSB], [https://www.ebi.ac.uk/pdbsum/4xgm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xgm ProSAT]</span></td></tr>
 </table>
+== Disease ==
+[https://www.uniprot.org/uniprot/MRPP3_HUMAN MRPP3_HUMAN] The disease is caused by variants affecting the gene represented in this entry.
 == Function ==
-[[http://www.uniprot.org/uniprot/MRRP3_HUMAN MRRP3_HUMAN]] Functions in mitochondrial tRNA maturation. Part of mitochondrial ribonuclease P, an enzyme composed of MRPP1/TRMT10C, MRPP2/HSD17B10 and MRPP3/KIAA0391, which cleaves tRNA molecules in their 5'-ends.<ref>PMID:18984158</ref>
+[https://www.uniprot.org/uniprot/MRPP3_HUMAN MRPP3_HUMAN] Catalytic ribonuclease component of mitochondrial ribonuclease P, a complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and PRORP/MRPP3, which cleaves tRNA molecules in their 5'-ends (PubMed:18984158, PubMed:25953853, PubMed:34715011). The presence of TRMT10C/MRPP1, HSD17B10/MRPP2 is required to catalyze tRNA molecules in their 5'-ends (PubMed:25953853).<ref>PMID:18984158</ref> <ref>PMID:25953853</ref> <ref>PMID:34715011</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Mitochondrial RNA polymerase produces long polycistronic precursors that contain the mRNAs, rRNAs and tRNAs needed for mitochondrial translation. Mitochondrial RNase P (mt-RNase P) initiates the maturation of the precursors by cleaving at the 5' ends of the tRNAs. Human mt-RNase P is only active as a tripartite complex (mitochondrial RNase P proteins 1-3; MRPP1-3), whereas plant and trypanosomal RNase Ps (PRORPs)-albeit homologous to MRPP3-are active as single proteins. The reason for this discrepancy has so far remained obscure. Here, we present the crystal structure of human MRPP3, which features a remarkably distorted and hence non-productive active site that we propose will switch to a fully productive state only upon association with MRPP1, MRPP2 and pre-tRNA substrate. We suggest a mechanism in which MRPP1 and MRPP2 both deliver the pre-tRNA substrate and activate MRPP3 through an induced-fit process.
+Structure of the nuclease subunit of human mitochondrial RNase P.,Reinhard L, Sridhara S, Hallberg BM Nucleic Acids Res. 2015 May 7. pii: gkv481. PMID:25953853<ref>PMID:25953853</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4xgm" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Ribonuclease P]]
+[[Category: Homo sapiens]]
-[[Category: Hallberg, B M]]
+[[Category: Large Structures]]
-[[Category: Reinhard, L]]
+[[Category: Hallberg BM]]
-[[Category: Sridhara, S]]
+[[Category: Reinhard L]]
-[[Category: Hydrolase]]
+[[Category: Sridhara S]]
-[[Category: Metallonuclease]]
-[[Category: Mitochondria]]
-[[Category: Ppr domain]]
-[[Category: Rnase p]]
-[[Category: Zinc binding domain]]