4rou

Auto-inhibition Mechanism of Human Mitochondrial RNase P Protein ComplexAuto-inhibition Mechanism of Human Mitochondrial RNase P Protein Complex

Structural highlights

4rou is a 2 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 2.713Å
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]

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

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OCA

[1] 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

[2] 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

[3] 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

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