期刊
FEBS LETTERS
卷 535, 期 1-3, 页码 94-100出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(02)03880-2
关键词
nuclear magnetic resonance; small protein B; tmRNA; trans-translation; RNA-binding protein; extended oligonucleotide binding fold
Small protein B (SmpB) is required for trans-translation, binding specifically to tmRNA. We show here the solution structure of SmpB from an extremely thermophilic bacterium, Thermus thermophilus HB8, determined by heteronuclear nuclear magnetic resonance methods. The core of the protein consists of an antiparallel beta-barrel twisted up from eight beta-strands, each end of which is capped with the second or third helix, and the first helix is located beside the barrel. Its C-terminal sequence (20 residues), which is rich in basic residues, shows a poorly structured form, as often seen in isolated ribosomal proteins. The results are discussed in relation to the oligonucleotide binding fold. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据