1HW2: Fadr-Dna Complex: Transcriptional Control Of Fatty Acid Metabolism In Echerichia Coli

Citation:
Abstract
In Escherichia coli, the expression of fatty acid metabolic genes is controlled by the transcription factor, FadR. The affinity of FadR for DNA is controlled by long chain acyl-CoA molecules, which bind to the protein and modulate gene expression. The crystal structure of FadR reveals a two domain dimeric molecule where the N-terminal domains bind DNA, and the C-terminal domains bind acyl-CoA. The DNA binding domain has a winged-helix motif, and the C-terminal domain resembles the sensor domain of the Tet repressor. The FadR.DNA complex reveals how the protein interacts with DNA and specifically recognizes a palindromic sequence. Structural and functional similarities to the Tet repressor and the BmrR transcription factors suggest how the binding of the acyl-CoA effector molecule to the C-terminal domain may affect the DNA binding affinity of the N-terminal domain. We suggest that the binding of acyl-CoA disrupts a buried network of charged and polar residues in the C-terminal domain, and the resulting conformational change is transmitted to the N-terminal domain via a domain-spanning alpha-helix.
PDB ID: 1HW2Download
MMDB ID: 72321
PDB Deposition Date: 2001/1/9
Updated in MMDB: 2011/06
Experimental Method:
x-ray diffraction
Resolution: 3.25  Å
Source Organism:
synthetic construct
Similar Structures:
Biological Unit for 1HW2: tetrameric; determined by author
Molecular Components in 1HW2
Label Count Molecule
Proteins (2 molecules)
2
Fatty Acid Metabolism Regulator Protein(Gene symbol: fadR)
Molecule annotation
Nucleotides(2 molecules)
1
5'- D(*cp*gp*ap*tp*cp*tp*gp*gp*tp*cp*cp*gp*ap*cp*cp*ap*gp*ap*tp *gp*cp*t)-3'
Molecule annotation
1
5'- D(*g*cp*ap*tp*cp*tp*gp*gp*tp*cp*gp*gp*ap*cp*cp*ap*gp*ap*tp* Cp*gp*a)-3'
Molecule annotation
Chemical (1 molecule)
1
1
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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