4xgm: Difference between revisions
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==Structure of the nuclease subunit of human mitochondrial RNase P (MRPP3) at 1.98A== | ==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]] 1.98Å' scene=''> | <StructureSection load='4xgm' size='340' side='right'caption='[[4xgm]], [[Resolution|resolution]] 1.98Å' scene=''> | ||
== Structural highlights == | == 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 [http://en.wikipedia.org/wiki/Human Human]. 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> | ||
</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='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> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KIAA0391, MRPP3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4xgm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xgm OCA], [http://pdbe.org/4xgm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xgm RCSB], [http://www.ebi.ac.uk/pdbsum/4xgm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xgm ProSAT]</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=4xgm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xgm OCA], [http://pdbe.org/4xgm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xgm RCSB], [http://www.ebi.ac.uk/pdbsum/4xgm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xgm ProSAT]</span></td></tr> | ||
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</div> | </div> | ||
<div class="pdbe-citations 4xgm" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4xgm" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Ribonuclease|Ribonuclease]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | |||
[[Category: Large Structures]] | |||
[[Category: Ribonuclease P]] | [[Category: Ribonuclease P]] | ||
[[Category: Hallberg, B M]] | [[Category: Hallberg, B M]] | ||
Revision as of 10:02, 29 May 2019
Structure of the nuclease subunit of human mitochondrial RNase P (MRPP3) at 1.98AStructure of the nuclease subunit of human mitochondrial RNase P (MRPP3) at 1.98A
Structural highlights
Function[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.[1] Publication Abstract from PubMedMitochondrial 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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