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2q7f

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(New page: 200px<br /><applet load="2q7f" size="350" color="white" frame="true" align="right" spinBox="true" caption="2q7f, resolution 2.49&Aring;" /> '''Crystal structure of...)
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==Overview==
==Overview==
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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.
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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==
==About this Structure==
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==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17624311 17624311]
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17624311 17624311]
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: yrrb]]
[[Category: yrrb]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:18:04 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:36:50 2008''

Revision as of 16:36, 21 February 2008

Image:2q7f.jpg

2q7f, resolution 2.49Å

Drag the structure with the mouse to rotate

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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