Protein Structure from Scientific Research

Criteria that define hydrolysis-active conformations 15, amended for p97. (i) A water molecule next to the terminal phosphate (dark green) forms a hydrogen bond to the E305 side chain (dark blue). This lytic water molecule is polarized and thus activated for attack. (ii) R359 polarizes the γ-phosphate and is poised to hydrogen-bond after cleavage (light blue). (iii) The γ-phosphate is held in place by N348 via a hydrogen bond (black). Simulations of the N348Q mutant lack hydrolysis-active conformations due to steric hindrance from the longer Q side chain.

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