1e2x
From Proteopedia
(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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| - | [[Image:1e2x.gif|left|200px]]<br /><applet load="1e2x" size=" | + | [[Image:1e2x.gif|left|200px]]<br /><applet load="1e2x" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1e2x, resolution 2.00Å" /> | caption="1e2x, resolution 2.00Å" /> | ||
'''FADR, FATTY ACID RESPONSIVE TRANSCRIPTION FACTOR FROM E. COLI'''<br /> | '''FADR, FATTY ACID RESPONSIVE TRANSCRIPTION FACTOR FROM E. COLI'''<br /> | ||
==Overview== | ==Overview== | ||
| - | FadR is a dimeric acyl coenzyme A (acyl CoA)-binding protein and | + | 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== | ==About this Structure== | ||
| - | 1E2X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1E2X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E2X OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Aalten, D | + | [[Category: Aalten, D M.F Van.]] |
[[Category: Dirusso, C.]] | [[Category: Dirusso, C.]] | ||
[[Category: Knudsen, J.]] | [[Category: Knudsen, J.]] | ||
| - | [[Category: Wierenga, R | + | [[Category: Wierenga, R K.]] |
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: transcriptional regulation]] | [[Category: transcriptional regulation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:23:12 2008'' |
Revision as of 10:23, 21 February 2008
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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 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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