1E2X

FadR, fatty acid responsive transcription factor from E. coli

Summary for 1E2X

• Entry DOI: 10.2210/pdb1e2x/pdb
• Descriptor: FATTY ACID METABOLISM REGULATOR PROTEIN, SULFATE ION (3 entities in total)
• Functional Keywords: transcriptional regulation
• Biological source: ESCHERICHIA COLI
• Cellular location: Cytoplasm (Potential): P09371
• Total number of polymer chains: 1
• Total formula weight: 27685.24

Authors

Van Aalten, D.M.F.,Dirusso, C.C.,Knudsen, J.,Wierenga, R.K. (deposition date: 2000-05-30, release date: 2000-12-03, Last modification date: 2024-05-08)

Primary citation

Van Aalten, D.M.F.,Dirusso, C.C.,Knudsen, J.,Wierenga, R.K.
Crystal Structure of Fadr, a Fatty Acid-Responsive Transcription Factor with a Novel Acyl Coenzyme A-Binding Fold
Embo J., 19:5167-, 2000

PubMed Abstract: FadR is a dimeric acyl coenzyme A (acyl CoA)-binding protein and transcription factor that regulates the expression of genes encoding fatty acid biosynthetic and degrading enzymes in Escherichia coli. Here, the 2.0 A crystal structure of full-length FadR is described, determined using multi-wavelength anomalous dispersion. The structure reveals a dimer and a two-domain fold, with DNA-binding and acyl-CoA-binding sites located in an N-terminal and C-terminal domain, respectively. The N-terminal domain contains a winged helix-turn-helix prokaryotic DNA-binding fold. Comparison with known structures and analysis of mutagenesis data delineated the site of interaction with DNA. The C-terminal domain has a novel fold, consisting of a seven-helical bundle with a crossover topology. Careful analysis of the structure, together with mutational and biophysical data, revealed a putative hydrophobic acyl-CoA-binding site, buried in the core of the seven-helical bundle. This structure aids in understanding FadR function at a molecular level, provides the first structural scaffold for the large GntR family of transcription factors, which are keys in the control of metabolism in bacterial pathogens, and could thus be a possible target for novel chemotherapeutic agents.

PubMed: 11013219
DOI: 10.1093/EMBOJ/19.19.5167

Experimental method

X-RAY DIFFRACTION (2 Å)