2Q7F

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

Summary for 2Q7F

• Entry DOI: 10.2210/pdb2q7f/pdb
• Descriptor: YrrB protein (2 entities in total)
• Functional Keywords: tpr, yrrb, protein binding
• Biological source: Bacillus subtilis
• Total number of polymer chains: 2
• Total formula weight: 54285.01

Authors

Oh, J.,Han, D.,Kim, K.,Lim, H. (deposition date: 2007-06-06, release date: 2007-08-07, Last modification date: 2024-02-21)

Primary citation

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., 360:784-790, 2007

PubMed 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.

PubMed: 17624311
DOI: 10.1016/j.bbrc.2007.06.129

Experimental method

X-RAY DIFFRACTION (2.49 Å)