Taylor Gal4 sandbox 2 - Revision history

Taylor Gal4 sandbox 2 - Revision history http://52.214.119.220/wiki/index.php?title=Taylor_Gal4_sandbox_2&action=history Revision history for this page on the wiki en MediaWiki 1.11.2 Thu, 09 Apr 2026 16:27:43 GMT Ann Taylor at 15:12, 25 October 2011 http://52.214.119.220/wiki/index.php?title=Taylor_Gal4_sandbox_2&diff=1304730&oldid=prev <p></p> <table style="background-color: white; color:black;"> <col class='diff-marker' /> <col class='diff-content' /> <col class='diff-marker' /> <col class='diff-content' /> <tr> <td colspan='2' style="background-color: white; color:black;">←Older revision</td> <td colspan='2' style="background-color: white; color:black;">Revision as of 15:12, 25 October 2011</td> </tr> <tr><td colspan="2" class="diff-lineno">Line 12:</td> <td colspan="2" class="diff-lineno">Line 12:</td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> <tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>A specific DNA complex of the 65-residue, N-terminal fragment of the yeast transcriptional activator, GAL4, has been analysed at 2.7 A resolution by X-ray crystallography. The protein binds as a dimer to a symmetrical 17-base-pair sequence. A small, Zn(2+)-containing domain recognizes a conserved CCG triplet at each end of the site through direct contacts with the major groove. A short coiled-coil dimerization element imposes 2-fold symmetry. A segment of extended polypeptide chain links the metal-binding module to the dimerization element and specifies the length of the site. The relatively open structure of the complex would allow another protein to bind coordinately with GAL4. </div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>A specific DNA complex of the 65-residue, N-terminal fragment of the yeast transcriptional activator, GAL4, has been analysed at 2.7 A resolution by X-ray crystallography. The protein binds as a dimer to a symmetrical 17-base-pair sequence. A small, <ins style="color: red; font-weight: bold; text-decoration: none;"><scene name='Taylor_Gal4_sandbox_2/Zn_binding/1'></ins>Zn(2+)-containing domain<ins style="color: red; font-weight: bold; text-decoration: none;"></scene> </ins>recognizes a conserved CCG triplet at each end of the site through direct contacts with the major groove. A short coiled-coil dimerization element imposes 2-fold symmetry. A segment of extended polypeptide chain links the metal-binding module to the dimerization element and specifies the length of the site. The relatively open structure of the complex would allow another protein to bind coordinately with GAL4. </div></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>==About this Structure==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>==About this Structure==</div></td></tr> </table> Tue, 25 Oct 2011 15:12:51 GMT Ann Taylor http://52.214.119.220/wiki/index.php/Talk:Taylor_Gal4_sandbox_2 Ann Taylor at 15:01, 25 October 2011 http://52.214.119.220/wiki/index.php?title=Taylor_Gal4_sandbox_2&diff=1304723&oldid=prev <p></p> <table style="background-color: white; color:black;"> <col class='diff-marker' /> <col class='diff-content' /> <col class='diff-marker' /> <col class='diff-content' /> <tr> <td colspan='2' style="background-color: white; color:black;">←Older revision</td> <td colspan='2' style="background-color: white; color:black;">Revision as of 15:01, 25 October 2011</td> </tr> <tr><td colspan="2" class="diff-lineno">Line 12:</td> <td colspan="2" class="diff-lineno">Line 12:</td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> <tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div><del style="color: red; font-weight: bold; text-decoration: none;"><!</del>-- </div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><ins style="color: red; font-weight: bold; text-decoration: none;">A specific DNA complex of the 65</ins>-<ins style="color: red; font-weight: bold; text-decoration: none;">residue, N</ins>-<ins style="color: red; font-weight: bold; text-decoration: none;">terminal fragment of the yeast transcriptional activator</ins>, <ins style="color: red; font-weight: bold; text-decoration: none;">GAL4</ins>, <ins style="color: red; font-weight: bold; text-decoration: none;">has been analysed </ins>at <ins style="color: red; font-weight: bold; text-decoration: none;">2</ins>.<ins style="color: red; font-weight: bold; text-decoration: none;">7 A resolution by X-ray crystallography</ins>. <ins style="color: red; font-weight: bold; text-decoration: none;">The protein binds as a dimer to a symmetrical 17-base-pair sequence. A small</ins>, <ins style="color: red; font-weight: bold; text-decoration: none;">Zn(2+)-containing domain recognizes a conserved CCG triplet at each end of the site through direct contacts with </ins>the <ins style="color: red; font-weight: bold; text-decoration: none;">major groove</ins>. <ins style="color: red; font-weight: bold; text-decoration: none;">A short coiled</ins>-<ins style="color: red; font-weight: bold; text-decoration: none;">coil dimerization element imposes 2</ins>-<ins style="color: red; font-weight: bold; text-decoration: none;">fold symmetry. A segment of extended polypeptide chain links the metal-binding module to the dimerization element and specifies the length of the site. The relatively open structure of the complex would allow another protein to bind coordinately with GAL4. </ins></div></td></tr> <tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div><del style="color: red; font-weight: bold; text-decoration: none;">The line below this paragraph</del>, <del style="color: red; font-weight: bold; text-decoration: none;">{{ABSTRACT_PUBMED_1557122}}</del>, <del style="color: red; font-weight: bold; text-decoration: none;">adds the Publication Abstract to the page </del></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div></div></td></tr> <tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div><del style="color: red; font-weight: bold; text-decoration: none;">(as it appears on PubMed </del>at <del style="color: red; font-weight: bold; text-decoration: none;">http://www</del>.<del style="color: red; font-weight: bold; text-decoration: none;">pubmed</del>.<del style="color: red; font-weight: bold; text-decoration: none;">gov)</del>, <del style="color: red; font-weight: bold; text-decoration: none;">where 1557122 is </del>the <del style="color: red; font-weight: bold; text-decoration: none;">PubMed ID number</del>.</div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div></div></td></tr> <tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>--<del style="color: red; font-weight: bold; text-decoration: none;">></del></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div></div></td></tr> <tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div><del style="color: red; font-weight: bold; text-decoration: none;">{{ABSTRACT_PUBMED_1557122}}</del></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div></div></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>==About this Structure==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>==About this Structure==</div></td></tr> </table> Tue, 25 Oct 2011 15:01:47 GMT Ann Taylor http://52.214.119.220/wiki/index.php/Talk:Taylor_Gal4_sandbox_2 Ann Taylor: New page: 200px <br /> {{STRUCTURE_1d66| PDB=1d66 | SCENE= }} <br /> <br /> ===DNA RECOGNITION BY GAL4: STRUCTURE OF A PROTEIN/DNA COMPLEX===<br /> <br /> <br /> <br /> {{ABSTRACT_PUBMED_1557122}}<br /> <br /> ==About this Structure==<br /> [[1d66]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D66 OCA]. <br /> <br /> ==See Also==<br /> *[[Hydrogen in macromolecular models]]<br /> <br /> ==Reference==<br /> <ref group="xtra">PMID:1557122</ref><references group="xtra"/><br /> [[Category: Saccharomyces cerevisiae]]<br /> [[Category: Carey, M.]]<br /> [[Category: Harrison, S C.]]<br /> [[Category: Marmorstein, R.]]<br /> [[Category: Ptashne, M.]]<br /> [[Category: Double helix]]<br /> [[Category: Protein-dna complex]]<br /> [[Category: Transcription/dna complex]]</div> Tue, 25 Oct 2011 15:00:27 GMT Ann Taylor http://52.214.119.220/wiki/index.php/Talk:Taylor_Gal4_sandbox_2