PDBsum entry 3wz0

Hydrolase

PDB id: 3wz0

Contents

Protein chains

206 a.a.

105 a.a.

Waters ×34

PDB id:

3wz0

Name:

Hydrolase

Title:

On archaeal homologs of the human rnase p proteins pop5 and rpp30 in the hyperthermophilic archaeon thermococcus kodakarensis

Structure:

Ribonuclease p protein component 3. Chain: e, f. Synonym: rnase p component 3, rpp30. Engineered: yes. Ribonuclease p protein component 2. Chain: c, a. Synonym: rnase p component 2, pop5. Engineered: yes

Source:

Thermococcus kodakarensis kod1. Organism_taxid: 69014. Gene: rnp3, tk1450. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: rnp2, tk1767. Expression_system_taxid: 562

Resolution:

2.79Å R-factor: 0.273 R-free: 0.318

Authors:

K.Suematsu,T.Ueda,T.Nakashima,Y.Kakuta,M.Kimura

Key ref:

K.Suematsu et al. (2015). On archaeal homologs of the human RNase P proteins Pop5 and Rpp30 in the hyperthermophilic archaeon Thermococcus kodakarensis. Biosci Biotechnol Biochem, 79, 952-959. PubMed id: 25704799 DOI: 10.1080/09168451.2014.1003130

Date:

11-Sep-14 Release date: 16-Sep-15

Protein chains

Q5JH47  (RNP3_THEKO) -  Ribonuclease P protein component 3 from Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)

Seq: 220 a.a.

Struc: 206 a.a.

Protein chains

Q5JJ62  (RNP2_THEKO) -  Ribonuclease P protein component 2 from Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)

Seq: 120 a.a.

Struc: 105 a.a.

Enzyme reactions

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

DOI no: 10.1080/09168451.2014.1003130

Biosci Biotechnol Biochem 79:952-959 (2015)

PubMed id: 25704799

On archaeal homologs of the human RNase P proteins Pop5 and Rpp30 in the hyperthermophilic archaeon Thermococcus kodakarensis.

K.Suematsu, T.Ueda, T.Nakashima, Y.Kakuta, M.Kimura.

ABSTRACT

The ribonuclease P (RNase P) proteins TkoPop5 and TkoRpp30, homologs of human Pop5 and Rpp30, respectively, in the hyperthermophilic archaeon Thermococcus kodakarensis were prepared and characterized with respect to pre-tRNA cleavage activity using the reconstitution system of the well-studied Pyrococcus horikoshii RNase P. The reconstituted particle containing TkoPop5 in place of the P. horikoshii counterpart PhoPop5 retained pre-tRNA cleavage activity comparable to that of the reconstituted P. horikoshii RNase P, while that containing TkoRpp30 instead of its corresponding protein PhoRpp30 had slightly lower activity than the P. horikoshii RNase P. Moreover, we determined crystal structures of TkoRpp30 alone and in complex with TkoPop5. Like their P. horikoshii counterparts, whose structures were solved previously, TkoRpp30 and TkoPop5 fold into TIM barrel and RRM-like fold, respectively. This finding demonstrates that RNase P proteins in T. kodakarensis and P. horikoshii are interchangeable and that their three-dimensional structures are highly conserved.