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Association of bmAANAT3 with acetyl-CoA and CoA followed by NMR.

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posted on 09.05.2017, 17:40 by Adam A. Aboalroub, Ashleigh B. Bachman, Ziming Zhang, Dimitra Keramisanou, David J. Merkler, Ioannis Gelis

(A) 15N-HSQC of bmAANAT3 in the free (blue) and acetyl-CoA-bound state (green). The very large number of signals affected by acetyl-CoA indicates that chemical shift perturbations do not solely report cofactor binding at the catalytic funnel, but also induced conformational changes to distal regions of the enzyme. (B) Expanded region of the 15N-HSQC of bmAANAT3 in the free-state (blue), after the addition of 0.5 (orange) or 1.0 (green) equivalents of acetyl-CoA, showing the concomitant disappearance and appearance of the signals for the free and bound states. (C) Expanded region from the NMR titration course of bmAANAT3 with CoA highlighting signals from residues that either do not exhibit any line broadening (L76) or broaden beyond detection at different points of the titration (R125, D161, A162 and L179).

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