TreeGrafter-generated GO annotations
Diverse MarR bacterial regulators of auxin catabolism in the plant microbiome.
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Demonstrated that iadD and iadE are the minimal gene pair necessary and sufficient for IAA degradation in Variovorax and heterologous E. coli.
"To test the necessity of these genes, we constructed knockout strains CL14 ΔiadDE and CL14 ΔiadCDE. Both lacked the ability to degrade IAA (Fig. 1d), demonstrating that iadD and iadE are necessary and sufficient for IAA degradation by Variovorax."
Structural and biochemical characterization of the key components of an auxin degradation operon from the rhizosphere bacterium Variovorax.
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Determined the 1.8 A crystal structure (PDB 7YLS) and 2.6 A cryo-EM structure (PDB 8H2T) of Variovorax paradoxus S110 IadD/IadE, showing that three IadE subunits form the stem base of the alpha3beta3 heterohexamer to scaffold the three catalytic IadD subunits.
"IadE is a single-domain protein, containing a twisted seven-stranded β-sheet and 3 α-helices, which may mainly serve as a scaffold protein contributing to proper assembly of the oligomeric enzyme complex."
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Showed that three IadE subunits form the stem and three IadD subunits form the cap of the mushroom-shaped heterohexamer.
"An overall mushroom-shaped heterohexamer composed of 3 IadE at the “stem” and 3 IadD in the “cap” was resolved (Fig 3C)."
UniProtKB record for C5CSP7 (C5CSP7_VARPS)
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Contains the aromatic-ring-hydroxylating dioxygenase beta subunit domain (Ring_hydroxyl_B, PF00866 / IPR000391).
"DR InterPro; IPR000391; Rng_hydr_dOase-bsu."