Crystal structure of E-coli YhbY:: A representative of a novel class of RNA binding proteins

被引:27
作者
Ostheimer, GJ
Barkan, A [1 ]
Matthews, BW
机构
[1] Univ Oregon, Inst Mol Biol, Eugene, OR 97403 USA
[2] Univ Oregon, Dept Chem, Eugene, OR 97403 USA
[3] Univ Oregon, Dept Biol, Eugene, OR 97403 USA
[4] Univ Oregon, Dept Phys, Eugene, OR 97403 USA
[5] Univ Oregon, Howard Hughes Med Inst, Eugene, OR 97403 USA
基金
美国国家科学基金会; 美国国家卫生研究院;
关键词
D O I
10.1016/S0969-2126(02)00886-9
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
E. coli YhbY belongs to a conserved family of hypothetical proteins represented in eubacteria, archaea, and plants (Pfam code UPF0044). Three maize proteins harboring UPF0044-like domains are required for chloroplast group 11 intron splicing, and bioinformatic data suggest a role for prokaryotic UPF0044 members in translation. The crystal structure of YhbY has been determined. YhbY has a fold similar to that of the C-terminal domain of translation initiation factor 3 (IF3C), which binds to 16S rRNA in the 30S ribosome. Modeling studies indicate that the same surface is highly basic in all members of UPF0044, suggesting a conserved RNA binding surface. Taken together, the evidence suggests that members of UPF0044 constitute a previously unrecognized class of RNA binding domain.
引用
收藏
页码:1593 / 1601
页数:9
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