Fig. 5: Additional density for atorvastatin in the ATP-binding region. | Nature Communications

Fig. 5: Additional density for atorvastatin in the ATP-binding region.

From: Cryo-electron microscopy reveals sequential binding and activation of Ryanodine Receptors by statin triplets

Fig. 5

A Cartoon model of the ATP-binding region and the neighboring transmembrane region of RyR1. Shown is one protomer (colors) and the pore-forming region of a neighboring protomer (gray). B Cryo-EM density map for the open RyR1+atorvastatin structure, contoured at 5.5σ. C corresponding density map for an open RyR1 structure with ATP (purple) bound to the pocket. D Superposition of the ATP binding regions of closed and open RyR1, both in complex with atorvastatin. One helix of the TaF (thumb and forefinger) domain moves towards the transmembrane region, and the extension of the S6 helix moves laterally away. E Corresponding superposition of the same region for an open RyR1 in complex with ATP and open RyR1 in complex with atorvastatin. A helix in the ‘thumb’ and the S6 extension helix also move away relative to the ATP complex, indicating that the size of the ATP binding pocket is larger in the presence of atorvastatin.

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