5gp9: Difference between revisions
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==Structural analysis of fatty acid degradation regulator FadR from Bacillus halodurans== | |||
<StructureSection load='5gp9' size='340' side='right'caption='[[5gp9]], [[Resolution|resolution]] 1.75Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5gp9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Alkalihalobacillus_halodurans_C-125 Alkalihalobacillus halodurans C-125]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GP9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GP9 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.755Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene></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=5gp9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gp9 OCA], [https://pdbe.org/5gp9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gp9 RCSB], [https://www.ebi.ac.uk/pdbsum/5gp9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gp9 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9K8A4_HALH5 Q9K8A4_HALH5] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
FadR is a fatty acyl-CoA dependent transcription factor that regulates genes encoding proteins involved in fatty-acid degradation and synthesis pathways. In this study, the crystal structures of Bacillus halodurans FadR, which belong to the TetR family, have been determined in three different forms: ligand-bound, ligand-free and DNA-bound at resolutions of 1.75, 2.05 and 2.80 A, respectively. Structural and functional data showed that B. halodurans FadR was bound to its operator site without fatty acyl-CoAs. Structural comparisons among the three different forms of B. halodurans FadR revealed that the movement of DNA binding domains toward the operator DNA was blocked upon binding of ligand molecules. These findings suggest that the TetR family FadR negatively regulates the genes involved in fatty acid metabolism by binding cooperatively to the operator DNA as a dimer of dimers. | |||
Structural basis of operator sites recognition and effector binding in the TetR family transcription regulator FadR.,Yeo HK, Park YW, Lee JY Nucleic Acids Res. 2017 Apr 20;45(7):4244-4254. doi: 10.1093/nar/gkx009. PMID:28160603<ref>PMID:28160603</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5gp9" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
*[[Tetracycline repressor protein 3D structures|Tetracycline repressor protein 3D structures]] | |||
*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Alkalihalobacillus halodurans C-125]] | |||
[[Category: Large Structures]] | |||
[[Category: Lee JY]] | |||
[[Category: Park YW]] | |||
[[Category: Yeo HK]] | |||
Latest revision as of 14:38, 2 August 2023
Structural analysis of fatty acid degradation regulator FadR from Bacillus haloduransStructural analysis of fatty acid degradation regulator FadR from Bacillus halodurans
Structural highlights
FunctionPublication Abstract from PubMedFadR is a fatty acyl-CoA dependent transcription factor that regulates genes encoding proteins involved in fatty-acid degradation and synthesis pathways. In this study, the crystal structures of Bacillus halodurans FadR, which belong to the TetR family, have been determined in three different forms: ligand-bound, ligand-free and DNA-bound at resolutions of 1.75, 2.05 and 2.80 A, respectively. Structural and functional data showed that B. halodurans FadR was bound to its operator site without fatty acyl-CoAs. Structural comparisons among the three different forms of B. halodurans FadR revealed that the movement of DNA binding domains toward the operator DNA was blocked upon binding of ligand molecules. These findings suggest that the TetR family FadR negatively regulates the genes involved in fatty acid metabolism by binding cooperatively to the operator DNA as a dimer of dimers. Structural basis of operator sites recognition and effector binding in the TetR family transcription regulator FadR.,Yeo HK, Park YW, Lee JY Nucleic Acids Res. 2017 Apr 20;45(7):4244-4254. doi: 10.1093/nar/gkx009. PMID:28160603[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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