1h9g: Difference between revisions
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'''FADR, FATTY ACID RESPONSIVE TRANSCRIPTION FACTOR FROM E. COLI, IN COMPLEX WITH MYRISTOYL-COA''' | {{Structure | ||
|PDB= 1h9g |SIZE=350|CAPTION= <scene name='initialview01'>1h9g</scene>, resolution 2.10Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=COA:COENZYME+A'>COA</scene> and <scene name='pdbligand=MYR:MYRISTIC ACID'>MYR</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''FADR, FATTY ACID RESPONSIVE TRANSCRIPTION FACTOR FROM E. COLI, IN COMPLEX WITH MYRISTOYL-COA''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1H9G is a [ | 1H9G 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=1H9G 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 11:34:05 2008'' | ||
Revision as of 09:34, 20 March 2008
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| 1h9g, resolution 2.10Å | |||||||||||||
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| Ligands: | COA and MYR | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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. 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 11:34:05 2008
