1h9g: Difference between revisions
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==FadR, FATTY ACID RESPONSIVE TRANSCRIPTION FACTOR FROM E. COLI, in complex with myristoyl-CoA== | |||
<StructureSection load='1h9g' size='340' side='right' caption='[[1h9g]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='1h9g' size='340' side='right' caption='[[1h9g]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1e2x|1e2x]], [[1hw1|1hw1]], [[1hw2|1hw2]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1e2x|1e2x]], [[1hw1|1hw1]], [[1hw2|1hw2]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1h9g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h9g RCSB], [http://www.ebi.ac.uk/pdbsum/1h9g PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1h9g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h9g RCSB], [http://www.ebi.ac.uk/pdbsum/1h9g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1h9g ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h9/1h9g_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h9/1h9g_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
Revision as of 12:21, 10 January 2018
FadR, FATTY ACID RESPONSIVE TRANSCRIPTION FACTOR FROM E. COLI, in complex with myristoyl-CoAFadR, FATTY ACID RESPONSIVE TRANSCRIPTION FACTOR FROM E. COLI, in complex with myristoyl-CoA
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedFadR 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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