2q7f
From Proteopedia
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'''Crystal structure of YrrB: a TPR protein with an unusual peptide-binding site''' | '''Crystal structure of YrrB: a TPR protein with an unusual peptide-binding site''' | ||
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[[Category: Lim, H.]] | [[Category: Lim, H.]] | ||
[[Category: Oh, J.]] | [[Category: Oh, J.]] | ||
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| - | [[Category: | + | [[Category: Tpr]] |
| - | [[Category: | + | [[Category: Yrrb]] |
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Revision as of 11:28, 4 May 2008
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 Page seeded by OCA on Sun May 4 14:28:52 2008
Categories: Bacillus subtilis | Single protein | Han, D. | Kim, K. | Lim, H. | Oh, J. | Protein binding | Tpr | Yrrb
