Summary information and primary citation
- PDB-id
-
1h9t;
DSSR-derived features in text and
JSON formats; DNAproDB
- Class
- transcriptional regulation
- Method
- X-ray (3.25 Å)
- Summary
- Fadr, fatty acid responsive transcription factor from
e. coli in complex with fadb operator
- Reference
-
Van Aalten DMF, Dirusso CC, Knudsen J (2001): "The
Structural Basis of Acyl Coenzyme A-Dependent Regulation
of the Transcription Factor Fadr." Embo J.,
20, 2041. doi: 10.1093/EMBOJ/20.8.2041.
- Abstract
- FadR is an acyl-CoA-responsive transcription factor,
regulating fatty acid biosynthetic and degradation genes in
Escherichia coli. The apo-protein binds DNA as a homodimer,
an interaction that is disrupted by binding of acyl-COA:
The recently described structure of apo-FadR shows a DNA
binding domain coupled to an acyl-CoA binding domain with a
novel fold, but does not explain how binding of the
acyl-CoA effector molecule > 30 A away from the DNA
binding site affects transcriptional regulation. Here, we
describe the structures of the FadR-operator and FadR-
myristoyl-CoA binary complexes. The FadR-DNA complex
reveals a novel winged helix-turn-helix protein-DNA
interaction, involving sequence-specific contacts from the
wing to the minor groove. Binding of acyl-CoA results in
dramatic conformational changes throughout the protein,
with backbone shifts up to 4.5 A. The net effect is a
rearrangement of the DNA binding domains in the dimer,
resulting in a change of 7.2 A in separation of the DNA
recognition helices and the loss of DNA binding, revealing
the molecular basis of acyl-CoA-responsive regulation.
