2q7f | pdb_00002q7f
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Crystal structure of YrrB: a TPR protein with an unusual peptide-binding site
Overview
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.
About this Structure
2Q7F is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
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
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