Crystal structure of YrrB: A TPR protein with an unusual peptide-binding site

• Published in: Biochemical and biophysical research communications Vol. 360; no. 4; pp. 784 - 790
• Main Authors: Han, Dohyun, Oh, Jongkil, Kim, Kyunggon, Lim, Hyosun, Kim, Youngsoo
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 07.09.2007
• Subjects: Amino Acid Sequence; Bacillus subtilis; Bacillus subtilis - chemistry; Bacterial Proteins - chemistry; Bacterial Proteins - metabolism; Binding Sites; Crystal structure; Crystallography, X-Ray; Molecular Sequence Data; Peptides - metabolism; Protein Conformation; Protein interaction; Repetitive Sequences, Amino Acid; Sequence Homology, Amino Acid; Tetratricopeptide repeat; TPR; YrrB; Tetratricopeptide repeat; YrrB; Protein interaction; TPR; Crystal structure
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/j.bbrc.2007.06.129

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 2.5 Å 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.