2fkd
From Proteopedia
(Difference between revisions)
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<StructureSection load='2fkd' size='340' side='right'caption='[[2fkd]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='2fkd' size='340' side='right'caption='[[2fkd]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2fkd]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2fkd]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_186 Escherichia virus 186]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FKD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FKD FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</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=2fkd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fkd OCA], [https://pdbe.org/2fkd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fkd RCSB], [https://www.ebi.ac.uk/pdbsum/2fkd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fkd 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=2fkd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fkd OCA], [https://pdbe.org/2fkd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fkd RCSB], [https://www.ebi.ac.uk/pdbsum/2fkd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fkd ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/RPC1_BP186 RPC1_BP186] Repressor of lysogeny. | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[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=2fkd ConSurf]. | </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=2fkd ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Bacteriophage lambda is a paradigm for understanding the role of cooperativity in gene regulation. Comparison of the regulatory regions of lambda and the unrelated temperate bacteriophage 186 provides insight into alternate ways to assemble functional genetic switches. The structure of the C-terminal domain of the 186 repressor, determined at 2.7 A resolution, reveals an unusual heptamer of dimers, consistent with presented genetic studies. In addition, the structure of a cooperativity mutant of the full-length 186 repressor, identified by genetic screens, was solved to 1.95 A resolution. These structures provide a molecular basis for understanding lysogenic regulation in 186. Whereas the overall fold of the 186 and lambda repressor monomers is remarkably similar, the way the two repressors cooperatively assemble is quite different and explains in part the differences in their regulatory activity. | ||
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| - | The structural basis of cooperative regulation at an alternate genetic switch.,Pinkett HW, Shearwin KE, Stayrook S, Dodd IB, Burr T, Hochschild A, Egan JB, Lewis M Mol Cell. 2006 Mar 3;21(5):605-15. PMID:16507359<ref>PMID:16507359</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2fkd" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Escherichia virus 186]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Lewis | + | [[Category: Lewis M]] |
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Current revision
Crystal Structure of the C-terminal domain of Bacteriophage 186 repressor
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