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. 2017 May 8;292(28):11650–11658. doi: 10.1074/jbc.M117.787176

Table 1.

Dissociation constants of Cbl-IIa/b riboswitches

Riboswitch KD1,Adoa KD1,Mea Krel1b KD2,Mea Krel2b
nm nm nm
env8Cbl-IIa >1e7c 6 ± 3 >2e5c 480 ± 40 >2000c
env4Cbl-IIa >1e7c 44 ± 23 >2e5c 3000 ± 1000 >300c
T. elongatus cbiX Cbl-IIa 2700 ± 400 17 ± 3 200 300 ± 70 7
A. marina hupE Cbl-IIa 6900 ± 100 510 ± 300 10
env62CblIIa 110 ± 20 56 ± 20 2
S. elongatus hupE Cbl-IIa 640 ± 50 3800 ± 3000 0.2
env127Cbl-IIa 200 ± 30 1000 ± 300 0.2
env47Cbl-IIa 440 ± 30 4200 ± 1000 0.1
env77Cbl-IIa 890 ± 200 7700 ± 2000 0.1
env50Cbl-IIa 6.2 ± 5.0 140 ± 10 0.04
E. faecalis eutG Cbl-IIb 100 ± 40 36,000 ± 20,000 0.003

a Binding affinities are shown as the average ± S.D. from three independent titrations. For env8Cbl-IIa, env4Cbl-IIa, and T. elongatus cbiX Cbl-IIa riboswitches, the values for KD1 and KD2 were calculated using a multiple ligand-binding model.

b Krel = (KD,Ado)/(KD,Me).

c The values are based upon an estimate of the minimum value for KD based upon the ITC measurements.