7e1l

<StructureSection load='7e1l' size='340' side='right'caption='[[7e1l]], [[Resolution|resolution]] 2.40&Aring;' scene=''>

<table><tr><td colspan='2'>[[7e1l]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7E1L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7E1L FirstGlance]. <br>

</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><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=7e1l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7e1l OCA], [https://pdbe.org/7e1l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7e1l RCSB], [https://www.ebi.ac.uk/pdbsum/7e1l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7e1l ProSAT]</span></td></tr>

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

The production of secondary metabolites is a major mechanism used by beneficial rhizobacteria to antagonize plant pathogens. These bacteria have evolved to coordinate the production of different secondary metabolites due to the heavy metabolic burden imposed by secondary metabolism. However, for most secondary metabolites produced by bacteria, it is not known how their biosynthesis is coordinated. Here, we showed that PhlH from the rhizobacterium Pseudomonas fluorescens is a TetR-family regulator coordinating the expression of enzymes related to the biosynthesis of several secondary metabolites, including 2,4-diacetylphloroglucinol (2,4-DAPG), mupirocin, and pyoverdine. We present structures of PhlH in both its apo form and 2,4-DAPG-bound form and elucidate its ligand-recognizing and allosteric switching mechanisms. Moreover, we found that dissociation of 2,4-DAPG from the ligand-binding domain of PhlH was sufficient to allosterically trigger a pendulum-like movement of the DNA-binding domains within the PhlH dimer, leading to a closed-to-open conformational transition. Finally, molecular dynamics simulations confirmed that two distinct conformational states were stabilized by specific hydrogen bonding interactions and that disruption of these hydrogen bonds had profound effects on the conformational transition. Our findings not only reveal a well-conserved route of allosteric signal transduction in TetR-family regulators but also provide novel mechanistic insights into bacterial metabolic coregulation.

Molecular basis for coordinating secondary metabolite production by bacterial and plant signaling molecules.,Zhang N, Wu J, Zhang S, Yuan M, Xu H, Li J, Zhang P, Wang M, Kempher ML, Tao X, Zhang LQ, Ge H, He YX J Biol Chem. 2022 Jun;298(6):102027. doi: 10.1016/j.jbc.2022.102027. Epub 2022, May 11. PMID:35568198<ref>PMID:35568198</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 7e1l" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Ge, H]]

[[Category: He, Y X]]

[[Category: Wu, J]]

[[Category: Zhang, N]]

[[Category: Transcription]]