2cax: Difference between revisions
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[[Image:2cax.gif|left|200px]] | [[Image:2cax.gif|left|200px]] | ||
'''STRUCTURAL BASIS FOR COOPERATIVE BINDING OF RIBBON-HELIX-HELIX REPRESSOR OMEGA TO MUTATED DIRECT DNA HEPTAD REPEATS''' | {{Structure | ||
|PDB= 2cax |SIZE=350|CAPTION= <scene name='initialview01'>2cax</scene>, resolution 2.90Å | |||
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|LIGAND= | |||
|ACTIVITY= | |||
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'''STRUCTURAL BASIS FOR COOPERATIVE BINDING OF RIBBON-HELIX-HELIX REPRESSOR OMEGA TO MUTATED DIRECT DNA HEPTAD REPEATS''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2CAX is a [ | 2CAX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CAX OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16528102 16528102] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptococcus pyogenes]] | [[Category: Streptococcus pyogenes]] | ||
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[[Category: Weihofen, W A.]] | [[Category: Weihofen, W A.]] | ||
[[Category: cooperative dna binding]] | [[Category: cooperative dna binding]] | ||
[[Category: direct | [[Category: direct repeat]] | ||
[[Category: dna heptad 5'-a/t atcac a/t - | [[Category: dna heptad 5'-a/t atcac a/t -3s']] | ||
[[Category: dna-binding]] | [[Category: dna-binding]] | ||
[[Category: inc18 family]] | [[Category: inc18 family]] | ||
[[Category: inc18 family of | [[Category: inc18 family of plasmid]] | ||
[[Category: inverted | [[Category: inverted repeat]] | ||
[[Category: metj/arc superfamily]] | [[Category: metj/arc superfamily]] | ||
[[Category: plasmid maintenance]] | [[Category: plasmid maintenance]] | ||
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[[Category: transcriptional repressor]] | [[Category: transcriptional repressor]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:13:05 2008'' |
Revision as of 17:13, 20 March 2008
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Coordinates: | save as pdb, mmCIF, xml |
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
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- Single protein
- Streptococcus pyogenes
- Alonso, J C.
- Cicek, A.
- Pratto, F.
- Saenger, W.
- Weihofen, W A.
- Cooperative dna binding
- Direct repeat
- Dna heptad 5'-a/t atcac a/t -3s'
- Dna-binding
- Inc18 family
- Inc18 family of plasmid
- Inverted repeat
- Metj/arc superfamily
- Plasmid maintenance
- Regulatory protein
- Rhh
- Ribbon-helix-helix
- Transcriptional repressor