1FBN
CRYSTAL STRUCTURE OF A FIBRILLARIN HOMOLOGUE FROM METHANOCOCCUS JANNASCHII, A HYPERTHERMOPHILE, AT 1.6 A
Summary for 1FBN
| Entry DOI | 10.2210/pdb1fbn/pdb |
| Descriptor | MJ FIBRILLARIN HOMOLOGUE (2 entities in total) |
| Functional Keywords | fibrillarin, mj proteins, ribosomal rna processing, snornp, structural genomics, bsgc structure funded by nih, protein structure initiative, psi, berkeley structural genomics center, ribosome |
| Biological source | Methanocaldococcus jannaschii |
| Total number of polymer chains | 1 |
| Total formula weight | 26239.73 |
| Authors | Wang, H.,Boisvert, D.,Kim, K.K.,Kim, R.,Kim, S.H.,Berkeley Structural Genomics Center (BSGC) (deposition date: 1999-04-25, release date: 2000-04-26, Last modification date: 2024-11-06) |
| Primary citation | Wang, H.,Boisvert, D.,Kim, K.K.,Kim, R.,Kim, S.H. Crystal structure of a fibrillarin homologue from Methanococcus jannaschii, a hyperthermophile, at 1.6 A resolution. EMBO J., 19:317-323, 2000 Cited by PubMed Abstract: Fibrillarin is a phylogenetically conserved protein essential for efficient processing of pre-rRNA through its association with a class of small nucleolar RNAs during ribosomal biogenesis. The protein is the antigen for the autoimmune disease scleroderma. Here we report the crystal structure of the fibrillarin homologue from Methanococcus jannaschii, a hyperthermophile, at 1.6 A resolution. The structure consists of two domains, with a novel fold in the N-terminal region and a methyltransferase-like domain in the C-terminal region. Mapping temperature-sensitive mutations found in yeast fibrillarin Nop1 to the Methanococcus homologue structure reveals that many of the mutations cluster in the core of the methyltransferase-like domain. PubMed: 10654930DOI: 10.1093/emboj/19.3.317 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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