Systematic Identification of Cyclic-di-GMP Binding Proteins in Vibrio cholerae Reveals a Novel Class of Cyclic-di-GMP-Binding ATPases Associated with Type II Secretion Systems
Fig 2
C-di-GMP bind to MshE ATPase with high affinity, specificity and independently of ATP.
(A) Fraction bound 32P-c-di-GMP to decreasing concentrations of purified His-MBP-MshE. The dissociation constant (Kd) is indicated. Fraction bound of His-MBP-MshE to (B) 32P-c-di-GMP and (C) 32P-ATP in the presence of 100 μM nucleotide competitors. P-value was determined by two-tailed t-test (*** p≤0.001). All data are average of three independent assays and standard deviation is indicated by error bars.