4XGL

Structure of the nuclease subunit of human mitochondrial RNase P (MRPP3) at 1.8A

Summary for 4XGL

• Entry DOI: 10.2210/pdb4xgl/pdb
• Descriptor: Mitochondrial ribonuclease P protein 3, ZINC ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: ppr domain, zinc binding domain, metallonuclease, rnase p, hydrolase
• Biological source: Homo sapiens (Human)
• Cellular location: Mitochondrion : O15091
• Total number of polymer chains: 1
• Total formula weight: 44370.12

Authors

Reinhard, L.,Sridhara, S.,Hallberg, B.M. (deposition date: 2014-12-31, release date: 2015-05-13, Last modification date: 2024-05-08)

Primary citation

Reinhard, L.,Sridhara, S.,Hallberg, B.M.
Structure of the nuclease subunit of human mitochondrial RNase P.
Nucleic Acids Res., 43:5664-5672, 2015

PubMed Abstract: 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.

PubMed: 25953853
DOI: 10.1093/nar/gkv481

Experimental method

X-RAY DIFFRACTION (1.8 Å)