1h9t
From Proteopedia
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|PDB= 1h9t |SIZE=350|CAPTION= <scene name='initialview01'>1h9t</scene>, resolution 3.25Å | |PDB= 1h9t |SIZE=350|CAPTION= <scene name='initialview01'>1h9t</scene>, resolution 3.25Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> | + | |LIGAND= <scene name='pdbligand=AU:GOLD+ION'>AU</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DA:2'-DEOXYADENOSINE-5'-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5'-MONOPHOSPHATE'>DT</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h9t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h9t OCA], [http://www.ebi.ac.uk/pdbsum/1h9t PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1h9t RCSB]</span> | ||
}} | }} | ||
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[[Category: Dirusso, C.]] | [[Category: Dirusso, C.]] | ||
[[Category: Knudsen, J.]] | [[Category: Knudsen, J.]] | ||
| - | [[Category: AU]] | ||
| - | [[Category: CL]] | ||
[[Category: transcriptional regulation]] | [[Category: transcriptional regulation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:00:43 2008'' |
Revision as of 18:00, 30 March 2008
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| , resolution 3.25Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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 Sun Mar 30 21:00:43 2008
