View source for 3ang


==Crystal structure of Thermus thermophilus FadR in complex with E. coli-derived dodecyl-CoA==
<StructureSection load='3ang' size='340' side='right'caption='[[3ang]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3ang]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ANG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ANG 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]] 2.25&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DCC:DODECYL-COA'>DCC</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=3ang FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ang OCA], [https://pdbe.org/3ang PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ang RCSB], [https://www.ebi.ac.uk/pdbsum/3ang PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ang ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q5SM42_THET8 Q5SM42_THET8] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In the extremely thermophilic bacterium Thermus thermophilus HB8, one of the four TetR family transcriptional regulators, which we named T. thermophilus FadR, negatively regulated the expression of several genes, including those involved in fatty acid degradation, both in vivo and in vitro. T. thermophilus FadR repressed the target gene expression by binding pseudopalindromic sequences covering the predicted -10 hexamers of their promoters, and medium to long straight-chain (C10-18) fatty acyl-CoA molecules were effective for transcriptional derepression. An X-ray crystal structure analysis revealed that T. thermophilus FadR bound one lauroyl (C12)-CoA molecule per FadR monomer, with its acyl chain moiety in the center of the FadR molecule, enclosed within a tunnel-like substrate-binding pocket surrounded by hydrophobic residues, and the CoA moiety interacting with basic residues on the protein surface. The growth of T. thermophilus HB8, with palmitic acid as the sole carbon source, increased the expression of FadR-regulated genes. These results indicate that in T. thermophilus HB8, medium to long straight-chain fatty acids can be used for metabolic energy under the control of FadR, although the major fatty acids found in this strain are iso- and anteiso-branched-chain (C15 and 17) fatty acids.

TetR family transcriptional repressor Thermus thermophilus FadR controls fatty acid degradation.,Agari Y, Agari K, Sakamoto K, Kuramitsu S, Shinkai A Microbiology. 2011 Feb 24. PMID:21349973<ref>PMID:21349973</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3ang" style="background-color:#fffaf0;"></div>

==See Also==
*[[Tetracycline repressor protein 3D structures|Tetracycline repressor protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermus thermophilus HB8]]
[[Category: Agari K]]
[[Category: Agari Y]]
[[Category: Kuramitsu S]]
[[Category: Sakamoto K]]
[[Category: Shinkai A]]