2cax: Difference between revisions

Revision as of 17:46, 21 February 2008

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

OverviewOverview

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 -->) in palindromic inverted, converging (--><--) or diverging (<---->) orientation and also, unique to omega2 and contrasting other RHH2 repressors, to non-palindromic direct (-->-->) repeats. Here we investigate with crystal structures how omega2 binds specifically to heptads in minimal operators with (-->-->) and (--><--) 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 (-->-->), approximately 0.6 A shorter in (--><--) but would be approximately 0.6 A longer in (<---->). These variations grade interactions between adjacent omega2 and explain modulations in cooperative binding affinity of omega2 to operators with different heptad orientations.

About this StructureAbout this Structure

2CAX 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

Page seeded by OCA on Thu Feb 21 16:46:44 2008

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OCA

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 ==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.
+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.
 ==About this Structure==
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 [[Category: Single protein]]
 [[Category: Streptococcus pyogenes]]
-[[Category: Alonso, J.C.]]
+[[Category: Alonso, J C.]]
 [[Category: Cicek, A.]]
 [[Category: Pratto, F.]]
 [[Category: Saenger, W.]]
-[[Category: Weihofen, W.A.]]
+[[Category: Weihofen, W A.]]
 [[Category: cooperative dna binding]]
 [[Category: direct repeats]]
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 [[Category: transcriptional repressor]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 18:39:41 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:46:44 2008''