2cax: Difference between revisions

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[[Image:2cax.gif|left|200px]]<br /><applet load="2cax" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2cax.gif|left|200px]]
caption="2cax, resolution 2.90&Aring;" />
 
'''STRUCTURAL BASIS FOR COOPERATIVE BINDING OF RIBBON-HELIX-HELIX REPRESSOR OMEGA TO MUTATED DIRECT DNA HEPTAD REPEATS'''<br />
{{Structure
|PDB= 2cax |SIZE=350|CAPTION= <scene name='initialview01'>2cax</scene>, resolution 2.90&Aring;
|SITE=
|LIGAND=
|ACTIVITY=
|GENE=
}}
 
'''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 [http://en.wikipedia.org/wiki/Single_protein 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].  
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=16528102 16528102]
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 repeats]]
[[Category: direct repeat]]
[[Category: dna heptad 5'-a/t atcac a/t -3']]
[[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 plasmids]]
[[Category: inc18 family of plasmid]]
[[Category: inverted repeats]]
[[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 Feb 21 16:46:44 2008''
''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

File:2cax.gif


PDB ID 2cax

Drag the structure with the mouse to rotate
, resolution 2.90Å
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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