2cax

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<StructureSection load='2cax' size='340' side='right'caption='[[2cax]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
<StructureSection load='2cax' size='340' side='right'caption='[[2cax]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2cax]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/"micrococcus_scarlatinae"_klein_1884 "micrococcus scarlatinae" klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CAX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CAX FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2cax]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CAX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CAX FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1irq|1irq]], [[2bnw|2bnw]], [[2bnz|2bnz]]</div></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2cax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cax OCA], [https://pdbe.org/2cax PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cax RCSB], [https://www.ebi.ac.uk/pdbsum/2cax PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cax ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2cax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cax OCA], [https://pdbe.org/2cax PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cax RCSB], [https://www.ebi.ac.uk/pdbsum/2cax PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cax ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q57468_STRPY Q57468_STRPY]
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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.
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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<ref>PMID:16528102</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2cax" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Micrococcus scarlatinae klein 1884]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Alonso, J C]]
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[[Category: Streptococcus pyogenes]]
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[[Category: Cicek, A]]
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[[Category: Synthetic construct]]
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[[Category: Pratto, F]]
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[[Category: Alonso JC]]
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[[Category: Saenger, W]]
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[[Category: Cicek A]]
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[[Category: Weihofen, W A]]
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[[Category: Pratto F]]
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[[Category: Cooperative dna binding]]
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[[Category: Saenger W]]
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[[Category: Dna heptad 5'- a/t atcac a/t -3ss']]
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[[Category: Weihofen WA]]
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[[Category: Dna- binding]]
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[[Category: Inc18 family of plasmid]]
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[[Category: Metj/arc superfamily]]
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[[Category: Plasmid maintenance]]
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[[Category: Regulatory protein]]
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[[Category: Rhh]]
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[[Category: Transcriptional repressor]]
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Revision as of 08:38, 7 February 2024

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

PDB ID 2cax

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