嗜热古菌詹氏甲烷球菌中一种纤维原蛋白同源物的晶体结构，分辨率为1.6埃。
Crystal structure of a fibrillarin homologue from Methanococcus jannaschii, a hyperthermophile, at 1.6 A resolution.
作者信息
Wang H, Boisvert D, Kim K K, Kim R, Kim S H
机构信息
Department of Chemistry, University of California, Berkeley, CA 94720, USA.
出版信息
EMBO J. 2000 Feb 1;19(3):317-23. doi: 10.1093/emboj/19.3.317.
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.
摘要
纤维原蛋白是一种在系统发育上保守的蛋白质，在核糖体生物发生过程中，通过与一类小核仁RNA结合，对前体rRNA的有效加工至关重要。该蛋白质是自身免疫性疾病硬皮病的抗原。在此，我们报道了嗜热古菌詹氏甲烷球菌中纤维原蛋白同源物的晶体结构，分辨率为1.6埃。该结构由两个结构域组成，N端区域具有新颖的折叠，C端区域具有类甲基转移酶结构域。将酵母纤维原蛋白Nop1中发现的温度敏感突变映射到甲烷球菌同源物结构上，发现许多突变聚集在类甲基转移酶结构域的核心。
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