1e2x: Difference between revisions

New page: left|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="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1e2x.gif|left|200px]]<br /><applet load="1e2x" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1e2x, resolution 2.00&Aring;" />
caption="1e2x, resolution 2.00&Aring;" />
'''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, 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.
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E2X OCA].  
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.M.F.Van.]]
[[Category: Aalten, D M.F Van.]]
[[Category: Dirusso, C.]]
[[Category: Dirusso, C.]]
[[Category: Knudsen, J.]]
[[Category: Knudsen, J.]]
[[Category: Wierenga, R.K.]]
[[Category: Wierenga, R K.]]
[[Category: SO4]]
[[Category: SO4]]
[[Category: transcriptional regulation]]
[[Category: transcriptional regulation]]


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