PDBsum entry 4xgl

Hydrolase

PDB id: 4xgl

Contents

Protein chain

342 a.a.

Ligands

GOL ×2

Metals

_ZN

Waters ×178

PDB id:

4xgl

Name:

Hydrolase

Title:

Structure of the nuclease subunit of human mitochondrial rnase p (mrpp3) at 1.8a

Structure:

Mitochondrial ribonuclease p protein 3. Chain: a. Fragment: unp residues 207-583. Synonym: mitochondrial rnase p protein 3. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: kiaa0391, mrpp3. Expressed in: escherichia coli krx. Expression_system_taxid: 1452720

Resolution:

1.80Å R-factor: 0.190 R-free: 0.228

Authors:

L.Reinhard,S.Sridhara,B.M.Hallberg

Key ref:

L.Reinhard et al. (2015). Structure of the nuclease subunit of human mitochondrial RNase P. Nucleic Acids Res, 43, 5664-5672. PubMed id: 25953853 DOI: 10.1093/nar/gkv481

Date:

31-Dec-14 Release date: 13-May-15

Protein chain

O15091  (MRPP3_HUMAN) -  Mitochondrial ribonuclease P catalytic subunit from Homo sapiens

Seq: 583 a.a.

Struc: 342 a.a.

Enzyme reactions

• Enzyme class: E.C.3.1.26.5 - ribonuclease P.
• Reaction: Endonucleolytic cleavage of RNA, removing 5'-extra-nucleotide from tRNA precursor.

DOI no: 10.1093/nar/gkv481

Nucleic Acids Res 43:5664-5672 (2015)

PubMed id: 25953853

Structure of the nuclease subunit of human mitochondrial RNase P.

L.Reinhard, S.Sridhara, B.M.Hällberg.

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.