3clc: Difference between revisions

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 <StructureSection load='3clc' size='340' side='right'caption='[[3clc]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3clc]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterobacter_sp. Enterobacter sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CLC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CLC FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3clc]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterobacter_sp._RFL1396 Enterobacter sp. RFL1396]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CLC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CLC FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">esp1396IC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=42895 Enterobacter sp.])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=3clc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3clc OCA], [https://pdbe.org/3clc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3clc RCSB], [https://www.ebi.ac.uk/pdbsum/3clc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3clc ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q8GGH0_9ENTR Q8GGH0_9ENTR]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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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=3clc ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Controller (C) proteins regulate the timing of the expression of restriction and modification (R-M) genes through a combination of positive and negative feedback circuits. A single dimer bound to the operator switches on transcription of the C-gene and the endonuclease gene; at higher concentrations, a second dimer bound adjacently switches off these genes. Here we report the first structure of a C protein-DNA operator complex, consisting of two C protein dimers bound to the native 35 bp operator sequence of the R-M system Esp1396I. The structure reveals a role for both direct and indirect DNA sequence recognition. The structure of the DNA in the complex is highly distorted, with severe compression of the minor groove resulting in a 50 degrees bend within each operator site, together with a large expansion of the major groove in the centre of the DNA sequence. Cooperative binding between dimers governs the concentration-dependent activation-repression switch and arises, in part, from the interaction of Glu25 and Arg35 side chains at the dimer-dimer interface. Competition between Arg35 and an equivalent residue of the sigma(70) subunit of RNA polymerase for the Glu25 site underpins the switch from activation to repression of the endonuclease gene.
-Structural analysis of the genetic switch that regulates the expression of restriction-modification genes.,McGeehan JE, Streeter SD, Thresh SJ, Ball N, Ravelli RB, Kneale GG Nucleic Acids Res. 2008 Aug;36(14):4778-87. Epub 2008 Jul 21. PMID:18644840<ref>PMID:18644840</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3clc" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Enterobacter sp]]
+[[Category: Enterobacter sp. RFL1396]]
 [[Category: Large Structures]]
-[[Category: Ball, N]]
+[[Category: Ball N]]
-[[Category: Kneale, G G]]
+[[Category: Kneale GG]]
-[[Category: McGeehan, J E]]
+[[Category: McGeehan JE]]
-[[Category: Ravelli, R B]]
+[[Category: Ravelli RB]]
-[[Category: Streeter, S D]]
+[[Category: Streeter SD]]
-[[Category: Thresh, S J]]
+[[Category: Thresh SJ]]
-[[Category: Dna-bending]]
-[[Category: Helix-turn-helix]]
-[[Category: Protein-dna complex]]
-[[Category: Transcription regulator-dna complex]]
-[[Category: Transcriptional regulator]]