S-Space College of Medicine/School of Medicine (의과대학/대학원) Program in Cancer Biology (협동과정-종양생물학전공) Journal Papers (저널논문_협동과정-종양생물학전공)
Crystal structure of YrrB: a TPR protein with an unusual peptide-binding site
- Han, Dohyun; Oh, Jongkil; Kim, Kyunggon; Lim, Hyosun; Kim, Youngsoo
- Issue Date
- Biochem Biophys Res Commun. 2007 Sep 7;360(4):784-90. Epub 2007 Jul 5.
- Amino Acid Sequence; Bacillus subtilis/chemistry; Bacterial Proteins/*chemistry/metabolism; Binding Sites; Crystallography, X-Ray; Molecular Sequence Data; Peptides/*metabolism; Protein Conformation; Repetitive Sequences, Amino Acid; Sequence Homology, Amino Acid
- YrrB is a hypothetical protein containing a tetratricopeptide repeat (TPR) domain from a Gram-positive bacterium, Bacillus subtilis. We determined YrrB structure in the C2 space group to 2.5A resolution, which is the first TPR structure of the Gram-positive bacterium B. subtilis. In contrast to other known TPR structures, the concave surface of the YrrB TPR domain is composed of the putative peptide-binding pocket lined with positively-charged residues. This unique charge distribution reveals that YrrB can interact with partner proteins via an unusual TPR-mediated interaction mode, compared to that of other TPR-containing structures. Functional annotation using genomics analysis suggested that YrrB may be an interacting mediator in the complex formation among RNA sulfuration components. No proteins containing a TPR domain have been identified in the biosynthesis of sulfur-containing biomolecules. Thus, YrrB could play a new role as a connecting module among those proteins in the conserved gene cluster for RNA sulfuration.
- 0006-291X (Print)
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