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

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Authors
Han, Dohyun; Oh, Jongkil; Kim, Kyunggon; Lim, Hyosun; Kim, Youngsoo
Issue Date
2007-07-13
Publisher
Wiley-Blackwell
Citation
Biochem Biophys Res Commun. 2007 Sep 7;360(4):784-90. Epub 2007 Jul 5.
Keywords
Amino Acid SequenceBacillus subtilis/chemistryBacterial Proteins/*chemistry/metabolismBinding SitesCrystallography, X-RayMolecular Sequence DataPeptides/*metabolismProtein ConformationRepetitive Sequences, Amino AcidSequence Homology, Amino Acid
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.
ISSN
0006-291X (Print)
Language
English
URI
http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6WBK-4P48623-3&_user=10&_rdoc=1&_fmt=&_orig=search&_sort=d&_docanchor=&view=c&_acct=C000050221&_version=1&_urlVersion=0&_userid=10&md5=842ac4e3b02bc01a6a714438ee40fa46

http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=17624311

https://hdl.handle.net/10371/27908
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College of Medicine/School of Medicine (의과대학/대학원)Program in Cancer Biology (협동과정-종양생물학전공)Journal Papers (저널논문_협동과정-종양생물학전공)
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