Solution structure of a tmRNA-binding protein, SmpB, from Thermus thermophilus.
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.
Someya
Tatsuhiko
T
Department of Industrial Chemistry, Faculty of Engineering, Chiba Institute of Technology, Chiba 275-0016, Japan.
Nameki
Nobukazu
N
Hosoi
Haruko
H
Suzuki
Sakura
S
Hatanaka
Hideki
H
Fujii
Michiko
M
Terada
Takaho
T
Shirouzu
Mikako
M
Inoue
Yorinao
Y
Shibata
Takehiko
T
Kuramitsu
Seiki
S
Yokoyama
Shigeyuki
S
Kawai
Gota
G
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D016601:RNA-Binding Proteins / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid; D012996:Solutions; D016963:Thermus thermophilus
D001426:Bacterial Proteins; D016601:RNA-Binding Proteins; D012996:Solutions; C430328:small protein B