2bnw: Difference between revisions

Revision as of 10:46, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2bnw.png

Template:STRUCTURE 2bnw

STRUCTURAL BASIS FOR COOPERATIVE BINDING OF RIBBON-HELIX-HELIX OMEGA REPRESSOR TO DIRECT DNA HEPTAD REPEATSSTRUCTURAL BASIS FOR COOPERATIVE BINDING OF RIBBON-HELIX-HELIX OMEGA REPRESSOR TO DIRECT DNA HEPTAD REPEATS

Template:ABSTRACT PUBMED 16528102

About this StructureAbout this Structure

2BNW is a Single protein structure of sequence from Streptococcus pyogenes. Full crystallographic information is available from OCA.

ReferenceReference

Structures of omega repressors bound to direct and inverted DNA repeats explain modulation of transcription., Weihofen WA, Cicek A, Pratto F, Alonso JC, Saenger W, Nucleic Acids Res. 2006 Mar 9;34(5):1450-8. Print 2006. PMID:16528102

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-'''STRUCTURAL BASIS FOR COOPERATIVE BINDING OF RIBBON-HELIX-HELIX OMEGA REPRESSOR TO DIRECT DNA HEPTAD REPEATS'''
+===STRUCTURAL BASIS FOR COOPERATIVE BINDING OF RIBBON-HELIX-HELIX OMEGA REPRESSOR TO DIRECT DNA HEPTAD REPEATS===
-==Overview==
+<!--
-Repressor omega regulates transcription of genes required for copy number control, accurate segregation and stable maintenance of inc18 plasmids hosted by Gram-positive bacteria. omega belongs to homodimeric ribbon-helix-helix (RHH2) repressors typified by a central, antiparallel beta-sheet for DNA major groove binding. Homodimeric omega2 binds cooperatively to promotors with 7 to 10 consecutive non-palindromic DNA heptad repeats (5'-(A)/(T)ATCAC(A)/(T)-3', symbolized by --&gt;) in palindromic inverted, converging (--&gt;&lt;--) or diverging (&lt;----&gt;) orientation and also, unique to omega2 and contrasting other RHH2 repressors, to non-palindromic direct (--&gt;--&gt;) repeats. Here we investigate with crystal structures how omega2 binds specifically to heptads in minimal operators with (--&gt;--&gt;) and (--&gt;&lt;--) repeats. Since the pseudo-2-fold axis relating the monomers in omega(2) passes the central C-G base pair of each heptad with approximately 0.3 A downstream offset, the separation between the pseudo-2-fold axes is exactly 7 bp in (--&gt;--&gt;), approximately 0.6 A shorter in (--&gt;&lt;--) but would be approximately 0.6 A longer in (&lt;----&gt;). These variations grade interactions between adjacent omega2 and explain modulations in cooperative binding affinity of omega2 to operators with different heptad orientations.
+The line below this paragraph, {{ABSTRACT_PUBMED_16528102}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16528102 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16528102}}
 ==About this Structure==
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 [[Category: Rhh]]
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