1FBN

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

1FBN の概要

• エントリーDOI: 10.2210/pdb1fbn/pdb
• 分子名称: MJ FIBRILLARIN HOMOLOGUE (2 entities in total)
• 機能のキーワード: fibrillarin, mj proteins, ribosomal rna processing, snornp, structural genomics, bsgc structure funded by nih, protein structure initiative, psi, berkeley structural genomics center, ribosome
• 由来する生物種: Methanocaldococcus jannaschii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26239.73

構造登録者

Wang, H.,Boisvert, D.,Kim, K.K.,Kim, R.,Kim, S.H.,Berkeley Structural Genomics Center (BSGC) (登録日: 1999-04-25, 公開日: 2000-04-26, 最終更新日: 2024-11-06)

主引用文献

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

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: 10654930
DOI: 10.1093/emboj/19.3.317

実験手法

X-RAY DIFFRACTION (1.6 Å)