2fkd
From Proteopedia
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| - | [[Image:2fkd.gif|left|200px]] | + | [[Image:2fkd.gif|left|200px]] |
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| - | '''Crystal Structure of the C-terminal domain of Bacteriophage 186 repressor''' | + | {{Structure |
| + | |PDB= 2fkd |SIZE=350|CAPTION= <scene name='initialview01'>2fkd</scene>, resolution 2.70Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= CI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=233894 Aeromonas phage 25]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal Structure of the C-terminal domain of Bacteriophage 186 repressor''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2FKD is a [ | + | 2FKD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aeromonas_phage_25 Aeromonas phage 25]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FKD OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16507359 16507359] |
[[Category: Aeromonas phage 25]] | [[Category: Aeromonas phage 25]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: repressor]] | [[Category: repressor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:53:30 2008'' |
Revision as of 14:53, 20 March 2008
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| , resolution 2.70Å | |||||||
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| Gene: | CI (Aeromonas phage 25) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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.
About this Structure
2FKD is a Single protein structure of sequence from Aeromonas phage 25. Full crystallographic information is available from OCA.
Reference
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
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