 |
PDBsum entry 2fkd
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Transcription regulator
|
PDB id
|
|
|
|
2fkd
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
The structural basis of cooperative regulation at an alternate genetic switch.
|
|
|
Authors
|
|
H.W.Pinkett,
K.E.Shearwin,
S.Stayrook,
I.B.Dodd,
T.Burr,
A.Hochschild,
J.B.Egan,
M.Lewis.
|
|
|
Ref.
|
|
Mol Cell, 2006,
21,
605-615.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
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.
|
|
|
|
|
|
|
|
Figure 1.
Figure 1. Comparison of the λ and 186 Switch Regions
|
|
Figure 2.
Figure 2. Structures of the CTD of λ and 186 Repressor
|
|
|
|
|
|
The above figures are
reprinted
by permission from Cell Press:
Mol Cell
(2006,
21,
605-615)
copyright 2006.
|
|
|
|
|
|
|
