2fkd: Difference between revisions

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[[Image:2fkd.~~gif~~|left|200px]]

[[Image:2fkd.png|left|200px]]

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~~'''~~Crystal Structure of the C-terminal domain of Bacteriophage 186 repressor~~'''~~

===Crystal Structure of the C-terminal domain of Bacteriophage 186 repressor===

~~==Overview==~~

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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~~.

The line below this paragraph, {{ABSTRACT_PUBMED_16507359}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 16507359 is the PubMed ID number.

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==About this Structure==

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[[Category: Regulation]]

[[Category: Repressor]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4 03~~:59:54 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:50:26 2008''

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-[[Image:2fkd.gif|left|200px]]
+{{Seed}}
+[[Image:2fkd.png|left|200px]]
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 {{STRUCTURE_2fkd|  PDB=2fkd  |  SCENE=  }}
-'''Crystal Structure of the C-terminal domain of Bacteriophage 186 repressor'''
+===Crystal Structure of the C-terminal domain of Bacteriophage 186 repressor===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16507359}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16507359 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16507359}}
 ==About this Structure==
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 [[Category: Regulation]]
 [[Category: Repressor]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 03:59:54 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:50:26 2008''