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. Author manuscript; available in PMC: 2015 Mar 4.
Published in final edited form as: Structure. 2014 Feb 13;22(3):397–408. doi: 10.1016/j.str.2013.12.018

Figure 1. Specificity and Affinity of DrrA Binding to PI(4)P.

Figure 1

(A) DrrA321–647 partitioning with sucrose-loaded POPC LUVs containing 3% of the indicated phosphoinositides at three lipid concentrations. Values and error bars are mean and SD (n = 3). Gels show representative supernatant (S) and pellet (P) fractions at the indicated lipid concentrations.

(B) SPR analysis of DrrA321–647 association with POPC LUVs containing 3% PI(4)P. Left: representative sensorgrams after curve alignment and reference subtraction. Right: equilibrium responses (Req) from the data on the left as a function of [DrrA321–647]. Solid and dotted lines are fitted quadratic and Langmuir binding models, respectively. RU, resonance units. See also Figure S1 and Table S1.

(C) Binding of WT DrrA321–647 to dibutyl PI(4)P (purple) and Ins(1,4)P2 (orange) determined by ITC at 20°C. Left: baseline-corrected titration data. Right, fitted 1:1 binding models. KD values are mean ± SD (n = 3 or 4).