1hw2: Difference between revisions

Revision as of 14:05, 21 February 2008

FADR-DNA COMPLEX: TRANSCRIPTIONAL CONTROL OF FATTY ACID METABOLISM IN ECHERICHIA COLI

OverviewOverview

In Escherichia coli, the expression of fatty acid metabolic genes is controlled by the transcription factor, FadR. The affinity of FadR for DNA is controlled by long chain acyl-CoA molecules, which bind to the protein and modulate gene expression. The crystal structure of FadR reveals a two domain dimeric molecule where the N-terminal domains bind DNA, and the C-terminal domains bind acyl-CoA. The DNA binding domain has a winged-helix motif, and the C-terminal domain resembles the sensor domain of the Tet repressor. The FadR.DNA complex reveals how the protein interacts with DNA and specifically recognizes a palindromic sequence. Structural and functional similarities to the Tet repressor and the BmrR transcription factors suggest how the binding of the acyl-CoA effector molecule to the C-terminal domain may affect the DNA binding affinity of the N-terminal domain. We suggest that the binding of acyl-CoA disrupts a buried network of charged and polar residues in the C-terminal domain, and the resulting conformational change is transmitted to the N-terminal domain via a domain-spanning alpha-helix.

About this StructureAbout this Structure

1HW2 is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

The FadR.DNA complex. Transcriptional control of fatty acid metabolism in Escherichia coli., Xu Y, Heath RJ, Li Z, Rock CO, White SW, J Biol Chem. 2001 May 18;276(20):17373-9. Epub 2001 Feb 13. PMID:11279025

Page seeded by OCA on Thu Feb 21 13:05:28 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1hw2.gif|left|200px]]<br /><applet load="1hw2" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1hw2.gif|left|200px]]<br /><applet load="1hw2" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1hw2, resolution 3.25&Aring;" />
 '''FADR-DNA COMPLEX: TRANSCRIPTIONAL CONTROL OF FATTY ACID METABOLISM IN ECHERICHIA COLI'''<br />
 ==Overview==
-In Escherichia coli, the expression of fatty acid metabolic genes is, controlled by the transcription factor, FadR. The affinity of FadR for DNA, is controlled by long chain acyl-CoA molecules, which bind to the protein, and modulate gene expression. The crystal structure of FadR reveals a two, domain dimeric molecule where the N-terminal domains bind DNA, and the, C-terminal domains bind acyl-CoA. The DNA binding domain has a, winged-helix motif, and the C-terminal domain resembles the sensor domain, of the Tet repressor. The FadR.DNA complex reveals how the protein, interacts with DNA and specifically recognizes a palindromic sequence., Structural and functional similarities to the Tet repressor and the BmrR, transcription factors suggest how the binding of the acyl-CoA effector, molecule to the C-terminal domain may affect the DNA binding affinity of, the N-terminal domain. We suggest that the binding of acyl-CoA disrupts a, buried network of charged and polar residues in the C-terminal domain, and, the resulting conformational change is transmitted to the N-terminal, domain via a domain-spanning alpha-helix.
+In Escherichia coli, the expression of fatty acid metabolic genes is controlled by the transcription factor, FadR. The affinity of FadR for DNA is controlled by long chain acyl-CoA molecules, which bind to the protein and modulate gene expression. The crystal structure of FadR reveals a two domain dimeric molecule where the N-terminal domains bind DNA, and the C-terminal domains bind acyl-CoA. The DNA binding domain has a winged-helix motif, and the C-terminal domain resembles the sensor domain of the Tet repressor. The FadR.DNA complex reveals how the protein interacts with DNA and specifically recognizes a palindromic sequence. Structural and functional similarities to the Tet repressor and the BmrR transcription factors suggest how the binding of the acyl-CoA effector molecule to the C-terminal domain may affect the DNA binding affinity of the N-terminal domain. We suggest that the binding of acyl-CoA disrupts a buried network of charged and polar residues in the C-terminal domain, and the resulting conformational change is transmitted to the N-terminal domain via a domain-spanning alpha-helix.
 ==About this Structure==
-HW2 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 MG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HW2 OCA].
+HW2 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=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HW2 OCA].
 ==Reference==
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 [[Category: Escherichia coli]]
 [[Category: Single protein]]
-[[Category: Heath, R.J.]]
+[[Category: Heath, R J.]]
 [[Category: Li, Z.]]
-[[Category: Rock, C.O.]]
+[[Category: Rock, C O.]]
-[[Category: White, S.W.]]
+[[Category: White, S W.]]
 [[Category: Xu, Y.]]
 [[Category: MG]]
@@ Line 23: / Line 23: @@
 [[Category: protein-dna complex]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:51:47 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:05:28 2008''