Solution structure of a tmRNA‐binding protein, SmpB, from Thermus thermophilus

FEBS Letters

Shirouzu, Mikako²  Fujii, Michiko³  Inoue, Yorinao¹  Shibata, Takehiko¹  Kawai, Gota³  Someya, Tatsuhiko³  Terada, Takaho²  Hosoi, Haruko²  Suzuki, Sakura²  Yokoyama, Shigeyuki²  Hatanaka, Hideki²  Kuramitsu, Seiki¹  Nameki, Nobukazu³ 

[1] Structurome Project, RIKEN Harima Institute at SPring-8, Hyogo 679-5148, Japan;Protein Research Group, RIKEN Genomic Sciences Center, Yokohama 230-0045, Japan;Department of Industrial Chemistry, Faculty of Engineering, Chiba Institute of Technology, Chiba 275-0016, Japan

关键词: Nuclear magnetic resonance;    Small protein B;    tmRNA;    Trans-translation;    RNA-binding protein;    Extended oligonucleotide binding fold;    EF-Tu;    elongation factor Tu;    SmpB;    small protein B;    rmsd;    root mean square deviation;    OB-fold;    oligonucleotide binding fold;   

DOI  :  10.1016/S0014-5793(02)03880-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 β-barrel twisted up from eight β-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.

【 授权许可】

Unknown