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| | ==Crystal structure of a transcriptional regulator FadR from Bacillus subtilis in complex with stearoyl-CoA== | | ==Crystal structure of a transcriptional regulator FadR from Bacillus subtilis in complex with stearoyl-CoA== |
| - | <StructureSection load='3whc' size='340' side='right' caption='[[3whc]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='3whc' size='340' side='right'caption='[[3whc]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3whc]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacsu Bacsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WHC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WHC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3whc]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacsu Bacsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WHC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WHC FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ST9:STEAROYL-COENZYME+A'>ST9</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ST9:STEAROYL-COENZYME+A'>ST9</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3whb|3whb]], [[1vi0|1vi0]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3whb|3whb]], [[1vi0|1vi0]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fadR, ysiA, BSU28550 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fadR, ysiA, BSU28550 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</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=3whc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3whc OCA], [http://pdbe.org/3whc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3whc RCSB], [http://www.ebi.ac.uk/pdbsum/3whc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3whc ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3whc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3whc OCA], [https://pdbe.org/3whc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3whc RCSB], [https://www.ebi.ac.uk/pdbsum/3whc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3whc ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FADR_BACSU FADR_BACSU]] Transcriptional regulator in fatty acid degradation. Represses transcription of genes required for fatty acid transport and beta-oxidation, including acdA, fadA, fadB, fadE, fadF, fadG, fadH, fadM, fadN, lcfA and lcfB. Binding of FadR to DNA is specifically inhibited by long chain fatty acyl-CoA compounds of 14-20 carbon atoms in length. | + | [[https://www.uniprot.org/uniprot/FADR_BACSU FADR_BACSU]] Transcriptional regulator in fatty acid degradation. Represses transcription of genes required for fatty acid transport and beta-oxidation, including acdA, fadA, fadB, fadE, fadF, fadG, fadH, fadM, fadN, lcfA and lcfB. Binding of FadR to DNA is specifically inhibited by long chain fatty acyl-CoA compounds of 14-20 carbon atoms in length. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Bacsu]] | | [[Category: Bacsu]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Fujihashi, M]] | | [[Category: Fujihashi, M]] |
| | [[Category: Miki, K]] | | [[Category: Miki, K]] |
| Structural highlights
Function
[FADR_BACSU] Transcriptional regulator in fatty acid degradation. Represses transcription of genes required for fatty acid transport and beta-oxidation, including acdA, fadA, fadB, fadE, fadF, fadG, fadH, fadM, fadN, lcfA and lcfB. Binding of FadR to DNA is specifically inhibited by long chain fatty acyl-CoA compounds of 14-20 carbon atoms in length.
Publication Abstract from PubMed
Bacillus subtilis FadR (FadRBs ), a member of the TetR family of bacterial transcriptional regulators, represses five fad operons including 15 genes, most of which are involved in beta-oxidation of fatty acids. FadRBs binds to the five FadRBs boxes in the promoter regions and the binding is specifically inhibited by long-chain (C14 -C20 ) acyl-CoAs, causing derepression of the fad operons. To elucidate the structural mechanism of this regulator, we have determined the crystal structures of FadRBs proteins prepared with and without stearoyl(C18 )-CoA. The crystal structure without adding any ligand molecules unexpectedly includes one small molecule, probably dodecyl(C12 )-CoA derived from the Escherichia coli host, in its homodimeric structure. Also, we successfully obtained the structure of the ligand-bound form of the FadRBs dimer by co-crystallization, in which two stearoyl-CoA molecules are accommodated, with the binding mode being essentially equivalent to that of dodecyl-CoA. Although the acyl-chain-binding cavity of FadRBs is mainly hydrophobic, a hydrophilic patch encompasses the C1-C10 carbons of the acyl chain. This accounts for the previous report that the DNA binding of FadRBs is specifically inhibited by the long-chain acyl-CoAs but not by the shorter ones. Structural comparison of the ligand-bound and unliganded subunits of FadRBs revealed three regions around residues 21-31, 61-76, and 106-119 that were substantially changed in response to the ligand binding, and particularly with respect to the movements of Leu108 and Arg109. Site-directed mutagenesis of these residues revealed that Arg109, but not Leu108, is a key residue for maintenance of the DNA-binding affinity of FadRBs . Proteins 2014. (c) 2013 Wiley Periodicals, Inc.
Structural characterization of a ligand-bound form of Bacillus subtilis FadR involved in the regulation of fatty acid degradation.,Fujihashi M, Nakatani T, Hirooka K, Matsuoka H, Fujita Y, Miki K Proteins. 2013 Dec 20. doi: 10.1002/prot.24496. PMID:24356978[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Fujihashi M, Nakatani T, Hirooka K, Matsuoka H, Fujita Y, Miki K. Structural characterization of a ligand-bound form of Bacillus subtilis FadR involved in the regulation of fatty acid degradation. Proteins. 2013 Dec 20. doi: 10.1002/prot.24496. PMID:24356978 doi:http://dx.doi.org/10.1002/prot.24496
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