1fbn

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Revision as of 12:40, 20 November 2007

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spinqualitylabelsall models 1fbn, resolution 1.6Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF A FIBRILLARIN HOMOLOGUE FROM METHANOCOCCUS JANNASCHII, A HYPERTHERMOPHILE, AT 1.6 A

Overview

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.

About this Structure

1FBN is a Single protein structure of sequence from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA.

Reference

Crystal structure of a fibrillarin homologue from Methanococcus jannaschii, a hyperthermophile, at 1.6 A resolution., Wang H, Boisvert D, Kim KK, Kim R, Kim SH, EMBO J. 2000 Feb 1;19(3):317-23. PMID:10654930

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