Structural highlights
Function
[YRRB_BACSU] Could be an interacting mediator in the complex formation among RNA sulfuration components, RNA processing components, and aminoacyl-tRNA synthetases.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Crystal structure of YrrB: a TPR protein with an unusual peptide-binding site.,Han D, Oh J, Kim K, Lim H, Kim Y Biochem Biophys Res Commun. 2007 Sep 7;360(4):784-90. Epub 2007 Jul 5. PMID:17624311[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Han D, Oh J, Kim K, Lim H, Kim Y. Crystal structure of YrrB: a TPR protein with an unusual peptide-binding site. Biochem Biophys Res Commun. 2007 Sep 7;360(4):784-90. Epub 2007 Jul 5. PMID:17624311 doi:10.1016/j.bbrc.2007.06.129
