1e2x
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(New page: 200px<br /><applet load="1e2x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e2x, resolution 2.00Å" /> '''FADR, FATTY ACID RES...)
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Revision as of 11:38, 20 November 2007
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FADR, FATTY ACID RESPONSIVE TRANSCRIPTION FACTOR FROM E. COLI
Overview
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.
About this Structure
1E2X is a Single protein structure of sequence from Escherichia coli with SO4 as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of FadR, a fatty acid-responsive transcription factor with a novel acyl coenzyme A-binding fold., van Aalten DM, DiRusso CC, Knudsen J, Wierenga RK, EMBO J. 2000 Oct 2;19(19):5167-77. PMID:11013219
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