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1k6o

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[[Image:1k6o.gif|left|200px]]<br /><applet load="1k6o" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1k6o, resolution 3.19&Aring;" />
 
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'''Crystal Structure of a Ternary SAP-1/SRF/c-fos SRE DNA Complex'''<br />
 
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==Overview==
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==Crystal Structure of a Ternary SAP-1/SRF/c-fos SRE DNA Complex==
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Combinatorial DNA binding by proteins for promoter-specific gene activation is a common mode of DNA regulation in eukaryotic organisms, and occurs at the promoter of the c-fos proto-oncogene. The c-fos promoter contains a serum response element (SRE) that mediates ternary complex formation with the Ets proteins SAP-1 or Elk-1 and the MADS-box protein, serum response factor (SRF). Here, we report the crystal structure of a ternary SAP-1/SRF/c-fos SRE DNA complex containing the minimal DNA-binding domains of each protein. The structure of the complex reveals that the SAP-1 monomer and SRF dimer are bound on opposite faces of the DNA, and that the DNA recognition helix of SAP-1 makes direct contact with the DNA recognition helix of one of the two SRF subunits. These interactions facilitate an 82 degrees DNA bend around SRF and a modulation of protein-DNA contacts by each protein when compared to each of the binary DNA complexes. A comparison with a recently determined complex containing SRF, an idealized DNA site, and a SAP-1 fragment containing a SRF-interacting B-box region, shows a similar overall architecture but also shows important differences. Specifically, the comparison suggests that the B-box region of the Ets protein does not significantly influence DNA recognition by either of the proteins, and that the sequence of the DNA target effects the way in which the two proteins cooperate for DNA recognition. These studies have implications for how DNA-bound SRF may modulate the DNA-binding properties of other Ets proteins such as Elk-1, and for how other Ets proteins may modulate the DNA-binding properties of other DNA-bound accessory factors to facilitate promoter-specific transcriptional responses.
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<StructureSection load='1k6o' size='340' side='right'caption='[[1k6o]], [[Resolution|resolution]] 3.19&Aring;' scene=''>
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== Structural highlights ==
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==Disease==
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<table><tr><td colspan='2'>[[1k6o]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K6O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K6O FirstGlance]. <br>
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Known disease associated with this structure: Osteoarthritis of hip, female-specific, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=605083 605083]]
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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]] 3.19&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1k6o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k6o OCA], [https://pdbe.org/1k6o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k6o RCSB], [https://www.ebi.ac.uk/pdbsum/1k6o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k6o ProSAT]</span></td></tr>
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==About this Structure==
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</table>
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1K6O is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K6O OCA].
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== Function ==
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[https://www.uniprot.org/uniprot/ELK4_HUMAN ELK4_HUMAN] Involved in both transcriptional activation and repression. Interaction with SIRT7 leads to recruitment and stabilization of SIRT7 at promoters, followed by deacetylation of histone H3 at 'Lys-18' (H3K18Ac) and subsequent transcription repression. Forms a ternary complex with the serum response factor (SRF). Requires DNA-bound SRF for ternary complex formation and makes extensive DNA contacts to the 5'side of SRF, but does not bind DNA autonomously.
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==Reference==
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== Evolutionary Conservation ==
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Crystal structure of a ternary SAP-1/SRF/c-fos SRE DNA complex., Mo Y, Ho W, Johnston K, Marmorstein R, J Mol Biol. 2001 Nov 30;314(3):495-506. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11846562 11846562]
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k6/1k6o_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1k6o ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Ho, W.]]
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[[Category: Ho W]]
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[[Category: Johnston, K.]]
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[[Category: Johnston K]]
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[[Category: Marmorstein, R.]]
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[[Category: Marmorstein R]]
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[[Category: Mo, Y.]]
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[[Category: Mo Y]]
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[[Category: combinatorial gene regulation]]
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[[Category: ets proteins]]
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[[Category: mads-box proteins]]
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[[Category: protein/dna complex]]
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[[Category: transcription factor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:30:41 2008''
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Current revision

Crystal Structure of a Ternary SAP-1/SRF/c-fos SRE DNA Complex

PDB ID 1k6o

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