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核糖体抗缔合因子IF6的晶体结构

Crystal structures of ribosome anti-association factor IF6.

作者信息

Groft C M, Beckmann R, Sali A, Burley S K

机构信息

Laboratories of Molecular Biophysics, The Rockefeller University, 1230 York Avenue, New York, New York 10021, USA.

出版信息

Nat Struct Biol. 2000 Dec;7(12):1156-64. doi: 10.1038/82017.

Abstract

Ribosome anti-association factor eIF6 (originally named according to translation initiation terminology as eukaryotic initiation factor 6) binds to the large ribosomal subunit, thereby preventing inappropriate interactions with the small subunit during initiation of protein synthesis. We have determined the X-ray structures of two IF6 homologs, Methanococcus jannaschii archaeal aIF6 and Sacchromyces cerevisiae eIF6, revealing a phylogenetically conserved 25 kDa protein consisting of five quasi identical alpha/beta subdomains arrayed about a five-fold axis of pseudosymmetry. Yeast eIF6 prevents ribosomal subunit association. Comparative protein structure modeling with other known archaeal and eukaryotic homologs demonstrated the presence of two conserved surface regions, one or both of which may bind the large ribosomal subunit.

摘要

核糖体抗缔合因子eIF6(最初根据翻译起始术语命名为真核起始因子6)与核糖体大亚基结合,从而在蛋白质合成起始过程中防止与小亚基发生不适当的相互作用。我们已经确定了两种IF6同源物的X射线结构,即詹氏甲烷球菌古菌aIF6和酿酒酵母eIF6,揭示了一种系统发育上保守的25 kDa蛋白质,它由围绕五重假对称轴排列的五个几乎相同的α/β亚结构域组成。酵母eIF6可防止核糖体亚基缔合。与其他已知的古菌和真核同源物进行的比较蛋白质结构建模表明,存在两个保守的表面区域,其中一个或两个区域可能与核糖体大亚基结合。

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