1e2x
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1e2x |SIZE=350|CAPTION= <scene name='initialview01'>1e2x</scene>, resolution 2.00Å | |PDB= 1e2x |SIZE=350|CAPTION= <scene name='initialview01'>1e2x</scene>, resolution 2.00Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e2x OCA], [http://www.ebi.ac.uk/pdbsum/1e2x PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1e2x RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Knudsen, J.]] | [[Category: Knudsen, J.]] | ||
[[Category: Wierenga, R K.]] | [[Category: Wierenga, R K.]] | ||
| - | [[Category: SO4]] | ||
[[Category: transcriptional regulation]] | [[Category: transcriptional regulation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:53:54 2008'' |
Revision as of 16:53, 30 March 2008
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| , resolution 2.00Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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