1PRY
Structure Determination of Fibrillarin Homologue From Hyperthermophilic Archaeon Pyrococcus furiosus (Pfu-65527)
Summary for 1PRY
| Entry DOI | 10.2210/pdb1pry/pdb |
| Descriptor | Fibrillarin-like pre-rRNA processing protein (2 entities in total) |
| Functional Keywords | structural genomics, fibrillarin, pyrococcus furiosus, snornp, ribosomal rna processing, methylation, pfu-65527, psi, protein structure initiative, southeast collaboratory for structural genomics, secsg, transferase |
| Biological source | Pyrococcus furiosus |
| Total number of polymer chains | 1 |
| Total formula weight | 25784.81 |
| Authors | Deng, L.,Starostina, N.G.,Liu, Z.-J.,Rose, J.P.,Terns, R.M.,Terns, M.P.,Wang, B.-C.,Southeast Collaboratory for Structural Genomics (SECSG) (deposition date: 2003-06-20, release date: 2004-03-09, Last modification date: 2024-02-14) |
| Primary citation | Deng, L.,Starostina, N.G.,Liu, Z.-J.,Rose, J.P.,Terns, R.M.,Terns, M.P.,Wang, B.-C.,Southeast Collaboratory for Structural Genomics Structure determination of fibrillarin from the hyperthermophilic archaeon Pyrococcus furiosus Biochem.Biophys.Res.Commun., 315:726-732, 2004 Cited by PubMed Abstract: The methyltransferase fibrillarin is the catalytic component of ribonucleoprotein complexes that direct site-specific methylation of precursor ribosomal RNA and are critical for ribosome biogenesis in eukaryotes and archaea. Here we report the crystal structure of a fibrillarin ortholog from the hyperthermophilic archaeon Pyrococcus furiosus at 1.97A resolution. Comparisons of the X-ray structures of fibrillarin orthologs from Methanococcus jannashii and Archaeoglobus fulgidus reveal nearly identical backbone configurations for the catalytic C-terminal domain with the exception of a unique loop conformation at the S-adenosyl-l-methionine (AdoMet) binding pocket in P. furiosus. In contrast, the N-terminal domains are divergent which may explain why some forms of fibrillarin apparently homodimerize (M. jannashii) while others are monomeric (P. furiosus and A. fulgidus). Three positively charged amino acids surround the AdoMet-binding site and sequence analysis indicates that this is a conserved feature of both eukaryotic and archaeal fibrillarins. We discuss the possibility that these basic residues of fibrillarin are important for RNA-guided rRNA methylation. PubMed: 14975761DOI: 10.1016/j.bbrc.2004.01.114 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.97 Å) |
Structure validation
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