View source for 6o6o


==Structure of the regulator FasR from Mycobacterium tuberculosis==
<StructureSection load='6o6o' size='340' side='right'caption='[[6o6o]], [[Resolution|resolution]] 1.63&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6o6o]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O6O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6O6O 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]] 1.63&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</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=6o6o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o6o OCA], [https://pdbe.org/6o6o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6o6o RCSB], [https://www.ebi.ac.uk/pdbsum/6o6o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6o6o ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O05858_MYCTU O05858_MYCTU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Mycobacterium tuberculosis is a pathogen with a unique cell envelope including very long fatty acids, implicated in bacterial resistance and host immune modulation. FasR is a TetR-like transcriptional activator that plays a central role in sensing mycobacterial long-chain fatty acids and regulating lipid biosynthesis. Here we disclose crystal structures of M. tuberculosis FasR in complex with acyl effector ligands and with DNA, uncovering its molecular sensory and switching mechanisms. A long tunnel traverses the entire effector-binding domain, enabling long fatty acyl effectors to bind. Only when the tunnel is entirely occupied, the protein dimer adopts a rigid configuration with its DNA-binding domains in an open state, leading to DNA dissociation. The protein-folding hydrophobic core connects the two domains, and is completed into a continuous spine when the effector binds. Such a transmission spine is conserved in a large number of TetR-like regulators, offering insight into effector-triggered allosteric functional control.

Mycobacterium tuberculosis FasR senses long fatty acyl-CoA through a tunnel and a hydrophobic transmission spine.,Lara J, Diacovich L, Trajtenberg F, Larrieux N, Malchiodi EL, Fernandez MM, Gago G, Gramajo H, Buschiazzo A Nat Commun. 2020 Jul 24;11(1):3703. doi: 10.1038/s41467-020-17504-x. PMID:32710080<ref>PMID:32710080</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6o6o" style="background-color:#fffaf0;"></div>

==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: Large Structures]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Buschiazzo A]]
[[Category: Gramajo H]]
[[Category: Lara J]]
[[Category: Larrieux N]]
[[Category: Trajtenberg F]]