1e2x: Difference between revisions
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'''FADR, FATTY ACID RESPONSIVE TRANSCRIPTION FACTOR FROM E. COLI''' | {{Structure | ||
|PDB= 1e2x |SIZE=350|CAPTION= <scene name='initialview01'>1e2x</scene>, resolution 2.00Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''FADR, FATTY ACID RESPONSIVE TRANSCRIPTION FACTOR FROM E. COLI''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1E2X is a [ | 1E2X is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E2X OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11013219 11013219] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transcriptional regulation]] | [[Category: transcriptional regulation]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:48:39 2008'' | ||
Revision as of 11:48, 20 March 2008
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FADR, FATTY ACID RESPONSIVE TRANSCRIPTION FACTOR FROM E. COLI
OverviewOverview
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 StructureAbout this Structure
1E2X is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
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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