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. 2013 Feb 5;33(2):e00022. doi: 10.1042/BSR20120115

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© 2013 The Author(s).

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial Licence (http://creativecommons.org/licenses/by-nc/2.5/) which permits unrestricted non-commercial use, distribution and reproduction in any medium, provided the original work is properly cited.

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(A) Structure of a portion of the wild-type PPIP5K2^KD catalytic centre [20] showing water molecules bridging the interaction between the ATP analogue AMPPNP (adenosine 5′-[β,γ-imido]triphosphate) and R213 and K248. (B) The effect of single-site mutants of PPIP5K2^KD on basal and InsP₆-stimulated (25 μM) ATPase activity. ATPase activity was measured as in Figure 8.