C-di-GMP bind to MshE ATPase with high affinity, specificity and independently of ATP.
- Kevin G. Roelofs (818861)
- Christopher J. Jones (531373)
- Sarah R. Helman (818862)
- Xiaoran Shang (818863)
- Mona W. Orr (818864)
- Jonathan R. Goodson (159318)
- Michael Y. Galperin (67366)
- Fitnat H. Yildiz (162562)
- Vincent T. Lee (42515)
Publication date
October 2015
DOIAbstract
<p>(A) Fraction bound <sup>32</sup>P-c-di-GMP to decreasing concentrations of purified His-MBP-MshE. The dissociation constant (K<sub>d</sub>) is indicated. Fraction bound of His-MBP-MshE to (B) <sup>32</sup>P-c-di-GMP and (C) <sup>32</sup>P-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.</p
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