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1hw1

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Revision as of 10:53, 27 September 2017

THE FADR-DNA COMPLEX: TRANSCRIPTIONAL CONTROL OF FATTY ACID METABOLISM IN ESCHERICHIA COLI

Structural highlights

1hw1 is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1hw2
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[FADR_ECOLI] Multifunctional regulator of fatty acid metabolism. Represses transcription of at least eight genes required for fatty acid transport and beta-oxidation including fadA, fadB, fadD, fadL and fadE. Activates transcription of at least three genes required for unsaturated fatty acid biosynthesis: fabA, fabB and iclR, the gene encoding the transcriptional regulator of the aceBAK operon encoding the glyoxylate shunt enzymes. Binding of FadR is specifically inhibited by long chain fatty acyl-CoA compounds.

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 PubMed

In Escherichia coli, the expression of fatty acid metabolic genes is controlled by the transcription factor, FadR. The affinity of FadR for DNA is controlled by long chain acyl-CoA molecules, which bind to the protein and modulate gene expression. The crystal structure of FadR reveals a two domain dimeric molecule where the N-terminal domains bind DNA, and the C-terminal domains bind acyl-CoA. The DNA binding domain has a winged-helix motif, and the C-terminal domain resembles the sensor domain of the Tet repressor. The FadR.DNA complex reveals how the protein interacts with DNA and specifically recognizes a palindromic sequence. Structural and functional similarities to the Tet repressor and the BmrR transcription factors suggest how the binding of the acyl-CoA effector molecule to the C-terminal domain may affect the DNA binding affinity of the N-terminal domain. We suggest that the binding of acyl-CoA disrupts a buried network of charged and polar residues in the C-terminal domain, and the resulting conformational change is transmitted to the N-terminal domain via a domain-spanning alpha-helix.

The FadR.DNA complex. Transcriptional control of fatty acid metabolism in Escherichia coli.,Xu Y, Heath RJ, Li Z, Rock CO, White SW J Biol Chem. 2001 May 18;276(20):17373-9. Epub 2001 Feb 13. PMID:11279025^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Xu Y, Heath RJ, Li Z, Rock CO, White SW. The FadR.DNA complex. Transcriptional control of fatty acid metabolism in Escherichia coli. J Biol Chem. 2001 May 18;276(20):17373-9. Epub 2001 Feb 13. PMID:11279025 doi:10.1074/jbc.M100195200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1hw1"

@@ Line 1: / Line 1: @@
 ==THE FADR-DNA COMPLEX: TRANSCRIPTIONAL CONTROL OF FATTY ACID METABOLISM IN ESCHERICHIA COLI==
 <StructureSection load='1hw1' size='340' side='right' caption='[[1hw1]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1hw1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HW1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HW1 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1hw1]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HW1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HW1 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1hw2|1hw2]]</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FADR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=1hw1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hw1 OCA], [http://pdbe.org/1hw1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hw1 RCSB], [http://www.ebi.ac.uk/pdbsum/1hw1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1hw1 ProSAT]</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=1hw1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hw1 OCA], [http://pdbe.org/1hw1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hw1 RCSB], [http://www.ebi.ac.uk/pdbsum/1hw1 PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 18: @@
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1hw1 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 33: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
 [[Category: Heath, R J]]
 [[Category: Li, Z]]

1hw1

From Proteopedia

Revision as of 10:53, 27 September 2017

THE FADR-DNA COMPLEX: TRANSCRIPTIONAL CONTROL OF FATTY ACID METABOLISM IN ESCHERICHIA COLI

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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