1h9t
From Proteopedia
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- | [[Image:1h9t.gif|left|200px]] | + | [[Image:1h9t.gif|left|200px]] |
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- | '''FADR, FATTY ACID RESPONSIVE TRANSCRIPTION FACTOR FROM E. COLI IN COMPLEX WITH FADB OPERATOR''' | + | {{Structure |
+ | |PDB= 1h9t |SIZE=350|CAPTION= <scene name='initialview01'>1h9t</scene>, resolution 3.25Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=AU:GOLD ION'>AU</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''FADR, FATTY ACID RESPONSIVE TRANSCRIPTION FACTOR FROM E. COLI IN COMPLEX WITH FADB OPERATOR''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1H9T is a [ | + | 1H9T is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H9T OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11296236 11296236] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transcriptional regulation]] | [[Category: transcriptional regulation]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:34:14 2008'' |
Revision as of 09:34, 20 March 2008
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, resolution 3.25Å | |||||||
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Ligands: | and | ||||||
Coordinates: | save as pdb, mmCIF, xml |
FADR, FATTY ACID RESPONSIVE TRANSCRIPTION FACTOR FROM E. COLI IN COMPLEX WITH FADB OPERATOR
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
1H9T is a Single protein structure of sequence from Escherichia coli. 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 Mar 20 11:34:14 2008