1h9g: Difference between revisions

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[[Image:1h9g.jpg|left|200px]]
[[Image:1h9g.jpg|left|200px]]


{{Structure
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{{STRUCTURE_1h9g| PDB=1h9g  | SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h9g OCA], [http://www.ebi.ac.uk/pdbsum/1h9g PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1h9g RCSB]</span>
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'''FADR, FATTY ACID RESPONSIVE TRANSCRIPTION FACTOR FROM E. COLI, IN COMPLEX WITH MYRISTOYL-COA'''
'''FADR, FATTY ACID RESPONSIVE TRANSCRIPTION FACTOR FROM E. COLI, IN COMPLEX WITH MYRISTOYL-COA'''
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[[Category: Dirusso, C.]]
[[Category: Dirusso, C.]]
[[Category: Knudsen, J.]]
[[Category: Knudsen, J.]]
[[Category: transcriptional regulation]]
[[Category: Transcriptional regulation]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 18:36:05 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:00:32 2008''

Revision as of 18:36, 2 May 2008

File:1h9g.jpg

Template:STRUCTURE 1h9g

FADR, FATTY ACID RESPONSIVE TRANSCRIPTION FACTOR FROM E. COLI, IN COMPLEX WITH MYRISTOYL-COA


OverviewOverview

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 StructureAbout this Structure

1H9G is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

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 Fri May 2 18:36:05 2008

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