title: Crystal structure of YrrB: a TPR protein with an unusual peptide-binding site.
abstract: 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.
authors.affiliation: College of Medicine, Seoul National University, Yongon-Dong, Seoul 110-799, Republic of Korea.
authors.forename: Dohyun
authors.initials: D
authors.lastname: Han
authors.forename: Jongkil
authors.initials: J
authors.lastname: Oh
authors.forename: Kyunggon
authors.initials: K
authors.lastname: Kim
authors.forename: Hyosun
authors.initials: H
authors.lastname: Lim
authors.forename: Youngsoo
authors.initials: Y
authors.lastname: Kim
mesh_terms: D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000737:chemistry; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D010455:Peptides / Q000378:metabolism*; D011487:Protein Conformation; D020449:Repetitive Sequences, Amino Acid; D017386:Sequence Homology, Amino Acid
chemical_list: D001426:Bacterial Proteins; D010455:Peptides