1H9T

FADR, FATTY ACID RESPONSIVE TRANSCRIPTION FACTOR FROM E. COLI IN COMPLEX WITH FADB OPERATOR

Summary for 1H9T

• Entry DOI: 10.2210/pdb1h9t/pdb
• Related: 1E2X 1H9G 1HW1 1HW2
• Descriptor: FATTY ACID METABOLISM REGULATOR PROTEIN, 5'-D(*CP*AP*TP*CP*TP*GP*GP*TP*AP*CP*GP*AP* CP*CP*AP*GP*AP*TP*C)-3', 5'-D(*GP*AP*TP*CP*TP*GP*GP*TP*CP*GP*TP*AP* CP*CP*AP*GP*AP*TP*G)-3', ... (6 entities in total)
• Functional Keywords: transcriptional regulation
• Biological source: ESCHERICHIA COLI
• Cellular location: Cytoplasm (Potential): P09371
• Total number of polymer chains: 4
• Total formula weight: 67137.07

Authors

Van Aalten, D.M.F.,Dirusso, C.C.,Knudsen, J. (deposition date: 2001-03-19, release date: 2001-04-04, Last modification date: 2023-12-13)

Primary citation

Van Aalten, D.M.F.,Dirusso, C.C.,Knudsen, J.
The Structural Basis of Acyl Coenzyme A-Dependent Regulation of the Transcription Factor Fadr
Embo J., 20:2041-, 2001

PubMed 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.

PubMed: 11296236
DOI: 10.1093/EMBOJ/20.8.2041

Experimental method

X-RAY DIFFRACTION (3.25 Å)