3WZ0
On archaeal homologs of the human RNase P proteins Pop5 and Rpp30 in the hyperthermophilic archaeon Thermococcus kodakarensis
Summary for 3WZ0
| Entry DOI | 10.2210/pdb3wz0/pdb |
| Related | 3WYZ |
| Descriptor | Ribonuclease P protein component 3, Ribonuclease P protein component 2 (3 entities in total) |
| Functional Keywords | tim barrel-like structure, rrm-like structure, pre-trna cleavage, hydrolase |
| Biological source | Thermococcus kodakarensis KOD1 More |
| Cellular location | Cytoplasm : Q5JH47 Q5JJ62 |
| Total number of polymer chains | 4 |
| Total formula weight | 78761.80 |
| Authors | Suematsu, K.,Ueda, T.,Nakashima, T.,Kakuta, Y.,Kimura, M. (deposition date: 2014-09-11, release date: 2015-09-16, Last modification date: 2024-03-20) |
| Primary citation | Suematsu, K.,Ueda, T.,Nakashima, T.,Kakuta, Y.,Kimura, M. On archaeal homologs of the human RNase P proteins Pop5 and Rpp30 in the hyperthermophilic archaeon Thermococcus kodakarensis. Biosci.Biotechnol.Biochem., 79:952-959, 2015 Cited by PubMed 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. PubMed: 25704799DOI: 10.1080/09168451.2014.1003130 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.79 Å) |
Structure validation
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