1pry

From Proteopedia

Revision as of 11:28, 20 March 2008

Structure Determination of Fibrillarin Homologue From Hyperthermophilic Archaeon Pyrococcus furiosus (Pfu-65527)

Overview

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.

About this Structure

1PRY is a Single protein structure of sequence from Pyrococcus furiosus. Full crystallographic information is available from OCA.

Reference

Structure determination of fibrillarin from the hyperthermophilic archaeon Pyrococcus furiosus., Deng L, Starostina NG, Liu ZJ, Rose JP, Terns RM, Terns MP, Wang BC, Biochem Biophys Res Commun. 2004 Mar 12;315(3):726-32. PMID:14975761

Page seeded by OCA on Thu Mar 20 13:28:13 2008