Fig. 6: Structure and mechanism for the allosteric regulation of SeXPK by ATP. | Nature Metabolism

Fig. 6: Structure and mechanism for the allosteric regulation of SeXPK by ATP.

From: An ATP-sensitive phosphoketolase regulates carbon fixation in cyanobacteria

Fig. 6

a, The dodecamer assembly of SeXPK in complex with 12 AMPPNP. b, Cross-section view of the XPK dimer unit showing 2 AMPPNP molecules (green spheres) bound to the dimer interface near the C terminus, whereas TPP/Mg2+ (yellow/green spheres) is located at the same interface but near the N terminus. c,d, A different view of the dimer interface for comparison between the free and complexed structures, respectively. e, Details of the ATP-binding site, showing that both AMPPNP molecules interact with residues from both subunits (pink and magenta colors). f, A bird’s eye view of the mechanism for allosteric inhibition in SeXPK. g–n, Stepwise illustration of the whole process of the allosteric regulation involving local conformational changes. Further explanation with a stereo views is provided in Extended Data Fig. 7. Primed residues designate residues from the reciprocal subunit in the dimer.

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