1J1H

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

Summary for 1J1H

• Entry DOI: 10.2210/pdb1j1h/pdb
• Descriptor: Small Protein B (1 entity in total)
• Functional Keywords: smpb, ssra associated protein, ob fold, riken structural genomics/proteomics initiative, rsgi, structural genomics, rna binding protein
• Biological source: Thermus thermophilus
• Cellular location: Cytoplasm (Potential): Q8RR57
• Total number of polymer chains: 1
• Total formula weight: 16785.49

Authors

Someya, T.,Nameki, N.,Hosoi, H.,Suzuki, S.,Hatanaka, H.,Fujii, M.,Terada, T.,Shirouzu, M.,Inoue, Y.,Shibata, T.,Kuramitsu, S.,Yokoyama, S.,Kawai, G.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2002-12-04, release date: 2003-02-11, Last modification date: 2023-12-27)

Primary citation

Someya, T.,Nameki, N.,Hosoi, H.,Suzuki, S.,Hatanaka, H.,Fujii, M.,Terada, T.,Shirouzu, M.,Inoue, Y.,Shibata, T.,Kuramitsu, S.,Yokoyama, S.,Kawai, G.
Solution structure of a tmRNA-binding protein, SmpB, from Thermus thermophilus
FEBS Lett., 535:94-100, 2003

PubMed Abstract: 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.

PubMed: 12560085
DOI: 10.1016/S0014-5793(02)03880-2

Experimental method

SOLUTION NMR