4xgm

From Proteopedia

(Difference between revisions)

Current revision

Structure of the nuclease subunit of human mitochondrial RNase P (MRPP3) at 1.98A

Structural highlights

4xgm is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.98Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

MRPP3_HUMAN The disease is caused by variants affecting the gene represented in this entry.

Function

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).^[1] ^[2] ^[3]

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^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Holzmann J, Frank P, Loffler E, Bennett KL, Gerner C, Rossmanith W. RNase P without RNA: identification and functional reconstitution of the human mitochondrial tRNA processing enzyme. Cell. 2008 Oct 31;135(3):462-74. PMID:18984158 doi:S0092-8674(08)01135-5
↑ Reinhard L, Sridhara S, Hallberg BM. Structure of the nuclease subunit of human mitochondrial RNase P. Nucleic Acids Res. 2015 May 7. pii: gkv481. PMID:25953853 doi:http://dx.doi.org/10.1093/nar/gkv481
↑ Hochberg I, Demain LAM, Richer J, Thompson K, Urquhart JE, Rea A, Pagarkar W, Rodríguez-Palmero A, Schlüter A, Verdura E, Pujol A, Quijada-Fraile P, Amberger A, Deutschmann AJ, Demetz S, Gillespie M, Belyantseva IA, McMillan HJ, Barzik M, Beaman GM, Motha R, Ng KY, O'Sullivan J, Williams SG, Bhaskar SS, Lawrence IR, Jenkinson EM, Zambonin JL, Blumenfeld Z, Yalonetsky S, Oerum S, Rossmanith W, Yue WW, Zschocke J, Munro KJ, Battersby BJ, Friedman TB, Taylor RW, O'Keefe RT, Newman WG. Bi-allelic variants in the mitochondrial RNase P subunit PRORP cause mitochondrial tRNA processing defects and pleiotropic multisystem presentations. Am J Hum Genet. 2021 Nov 4;108(11):2195-2204. PMID:34715011 doi:10.1016/j.ajhg.2021.10.002
↑ Reinhard L, Sridhara S, Hallberg BM. Structure of the nuclease subunit of human mitochondrial RNase P. Nucleic Acids Res. 2015 May 7. pii: gkv481. PMID:25953853 doi:http://dx.doi.org/10.1093/nar/gkv481

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4xgm"

Categories: Homo sapiens | Large Structures | Hallberg BM | Reinhard L | Sridhara S

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 4xgm is ON HOLD  until Paper Publication
+==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=''>
+== Structural highlights ==
+<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='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='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'>[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 ==
+[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.
-Authors: Reinhard, L., Sridhara, S., Hallberg, B.M.
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Hallberg, B.M]]
+<div class="pdbe-citations 4xgm" style="background-color:#fffaf0;"></div>
-[[Category: Sridhara, S]]
-[[Category: Reinhard, L]]
+==See Also==
+*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Hallberg BM]]
+[[Category: Reinhard L]]
+[[Category: Sridhara S]]

4xgm

From Proteopedia

Current revision

Structure of the nuclease subunit of human mitochondrial RNase P (MRPP3) at 1.98A

Structural highlights

Disease

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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