1h9g
From Proteopedia
(New page: 200px<br /><applet load="1h9g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h9g, resolution 2.10Å" /> '''FADR, FATTY ACID RES...) |
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| - | [[Image:1h9g.jpg|left|200px]]<br /><applet load="1h9g" size=" | + | [[Image:1h9g.jpg|left|200px]]<br /><applet load="1h9g" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1h9g, resolution 2.10Å" /> | caption="1h9g, resolution 2.10Å" /> | ||
'''FADR, FATTY ACID RESPONSIVE TRANSCRIPTION FACTOR FROM E. COLI, IN COMPLEX WITH MYRISTOYL-COA'''<br /> | '''FADR, FATTY ACID RESPONSIVE TRANSCRIPTION FACTOR FROM E. COLI, IN COMPLEX WITH MYRISTOYL-COA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | FadR is an acyl-CoA-responsive transcription factor, regulating fatty acid | + | FadR is an acyl-CoA-responsive transcription factor, regulating fatty acid biosynthetic and degradation genes in Escherichia coli. The apo-protein binds DNA as a homodimer, an interaction that is disrupted by binding of acyl-COA: The recently described structure of apo-FadR shows a DNA binding domain coupled to an acyl-CoA binding domain with a novel fold, but does not explain how binding of the acyl-CoA effector molecule > 30 A away from the DNA binding site affects transcriptional regulation. Here, we describe the structures of the FadR-operator and FadR- myristoyl-CoA binary complexes. The FadR-DNA complex reveals a novel winged helix-turn-helix protein-DNA interaction, involving sequence-specific contacts from the wing to the minor groove. Binding of acyl-CoA results in dramatic conformational changes throughout the protein, with backbone shifts up to 4.5 A. The net effect is a rearrangement of the DNA binding domains in the dimer, resulting in a change of 7.2 A in separation of the DNA recognition helices and the loss of DNA binding, revealing the molecular basis of acyl-CoA-responsive regulation. |
==About this Structure== | ==About this Structure== | ||
| - | 1H9G 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 COA and MYR as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1H9G 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=COA:'>COA</scene> and <scene name='pdbligand=MYR:'>MYR</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H9G 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.]] | ||
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[[Category: transcriptional regulation]] | [[Category: transcriptional regulation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:58:53 2008'' |
Revision as of 10:58, 21 February 2008
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FADR, FATTY ACID RESPONSIVE TRANSCRIPTION FACTOR FROM E. COLI, IN COMPLEX WITH MYRISTOYL-COA
Overview
FadR is an acyl-CoA-responsive transcription factor, regulating fatty acid biosynthetic and degradation genes in Escherichia coli. The apo-protein binds DNA as a homodimer, an interaction that is disrupted by binding of acyl-COA: The recently described structure of apo-FadR shows a DNA binding domain coupled to an acyl-CoA binding domain with a novel fold, but does not explain how binding of the acyl-CoA effector molecule > 30 A away from the DNA binding site affects transcriptional regulation. Here, we describe the structures of the FadR-operator and FadR- myristoyl-CoA binary complexes. The FadR-DNA complex reveals a novel winged helix-turn-helix protein-DNA interaction, involving sequence-specific contacts from the wing to the minor groove. Binding of acyl-CoA results in dramatic conformational changes throughout the protein, with backbone shifts up to 4.5 A. The net effect is a rearrangement of the DNA binding domains in the dimer, resulting in a change of 7.2 A in separation of the DNA recognition helices and the loss of DNA binding, revealing the molecular basis of acyl-CoA-responsive regulation.
About this Structure
1H9G is a Single protein structure of sequence from Escherichia coli with and as ligands. Full crystallographic information is available from OCA.
Reference
The structural basis of acyl coenzyme A-dependent regulation of the transcription factor FadR., van Aalten DM, DiRusso CC, Knudsen J, EMBO J. 2001 Apr 17;20(8):2041-50. PMID:11296236
Page seeded by OCA on Thu Feb 21 12:58:53 2008
