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. Author manuscript; available in PMC: 2013 Nov 25.
Published in final edited form as: Proteins. 2011 Oct 31;80(1):10.1002/prot.23186. doi: 10.1002/prot.23186

Figure 6.

Figure 6

A model of the role of His79 as a structural switch for the selectivity of enzymatic activity: Juxtaposition of “ATPase mode” and “AK mode.” According to the proposed ring-flip hypothesis, based on the structural analysis, the imidazole nitrogen ND1 of His79 can coordinate a lytic water molecule (together with the NZ of Lys16) during the ATPase reaction (ATP + H2O → ADP + Pi; ATPase-mode) or coordinate the α-phosphate of AMP (together with the NH1 of Arg39) during the reverse AK reaction (ATP + AMP → 2ADP; AK-mode; further details in the “Discussion” section).