2ZAE
Crystal structure of protein Ph1601p in complex with protein Ph1771p of archaeal ribonuclease P from Pyrococcus horikoshii OT3
Summary for 2ZAE
| Entry DOI | 10.2210/pdb2zae/pdb |
| Related | 1V76 1X0T |
| Descriptor | Ribonuclease P protein component 1, Ribonuclease P protein component 4, NITRATE ION, ... (6 entities in total) |
| Functional Keywords | ribonuclease p protein subunits, hetero dimer, hydrolase, trna processing |
| Biological source | Pyrococcus horikoshii More |
| Total number of polymer chains | 4 |
| Total formula weight | 60451.96 |
| Authors | Honda, T.,Kakuta, Y.,Kimura, M. (deposition date: 2007-10-04, release date: 2008-10-14, Last modification date: 2023-11-01) |
| Primary citation | Honda, T.,Kakuta, Y.,Kimura, K.,Saho, J.,Kimura, M. Structure of an archaeal homolog of the human protein complex Rpp21-Rpp29 that is a key core component for the assembly of active ribonuclease P. J.Mol.Biol., 384:652-662, 2008 Cited by PubMed Abstract: Ribonuclease P (RNase P) is a ribonucleoprotein complex involved in the processing of the 5'-leader sequence of precursor tRNA. Human RNase P protein subunits Rpp21 and Rpp29, which bind to each other, with catalytic RNA (H1 RNA) are sufficient for activating endonucleolytic cleavage of precursor tRNA. Here we have determined the crystal structure of the complex between the Pyrococcus horikoshii RNase P proteins PhoRpp21 and PhoRpp29, the archaeal homologs of Rpp21 and Rpp29, respectively. PhoRpp21 and PhoRpp29 form a heterodimeric structure where the two N-terminal helices (alpha1 and alpha2) in PhoRpp21 predominantly interact with the N-terminal extended structure, the beta-strand (beta2), and the C-terminal helix (alpha3) in PhoRpp29. The interface is dominated by hydrogen bonds and several salt bridges, rather than hydrophobic interactions. The electrostatic potential on the surface of the heterodimer shows a positively charged cluster on one face, suggesting a possible RNA-binding surface of the PhoRpp21-PhoRpp29 complex. The present structure, along with the result of a mutational analysis, suggests that heterodimerization between PhoRpp21 and PhoRpp29 plays an important role in the function of P. horikoshii RNase P. PubMed: 18929577DOI: 10.1016/j.jmb.2008.09.056 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.21 Å) |
Structure validation
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