Extended Data Fig. 4: Binding of 1″−3′-gcADPR by CbTad1.
From: Single phage proteins sequester signals from TIR and cGAS-like enzymes
a, Overall structure of CbTad1 hexamer bound to 1″−3′ gcADPR, which is shown as orange sticks. b, Detailed binding between CbTad1 and 1″−3′ gcADPR. Residues involved in 1″−3′ gcADPR binding are shown as sticks. Red dashed lines represent polar interactions. 2Fo-Fc electron density of 1″−3′ gcADPR within one binding pocket is shown and contoured at 1 σ. c, Native PAGE showed the binding of CbTad1 mutants to cA3 and 1″−2′ gcADPR. For gel source date, see Supplementary Fig. 1. d, ITC assays to test binding of cA3 to CbTad1 mutant. Representative binding curves and binding affinities are shown. The KD values are mean ± s.d. (n = 3 independent experiments). Raw data for these curves are shown in Supplementary Fig. 3.
