Crystal structure of YrrB: a TPR protein with an unusual peptide-binding site.
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.
Han
Dohyun
D
College of Medicine, Seoul National University, Yongon-Dong, Seoul 110-799, Republic of Korea.
Oh
Jongkil
J
Kim
Kyunggon
K
Lim
Hyosun
H
Kim
Youngsoo
Y
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
D001426:Bacterial Proteins; D010455:Peptides