Fig. 3: Function and structure of S-2L MazZ, a (d)GTP phosphohydrolase. | Nature Communications

Fig. 3: Function and structure of S-2L MazZ, a (d)GTP phosphohydrolase.

From: Characterization of a triad of genes in cyanophage S-2L sufficient to replace adenine by 2-aminoadenine in bacterial DNA

Fig. 3: Function and structure of S-2L MazZ, a (d)GTP phosphohydrolase.

a HPLC analysis of S-2L MazZ activity with dGTP and GTP (gold), with nucleotide standards below (black). b A tetramer of MazZ that constitutes the crystallographic asymmetric unit. Each catalytic pocket contains the reactant (lime) and three catalytic ions and results from interactions at the interface of two chains of a tight dimer. c A close-up on the catalytic pocket, in two views. The product of dGTP dephosphorylation (lime) is identified as dGDP in the crystal, next to three catalytic Mn2+ ions (lilac spheres). The determinants of guanine specificity (yellow for N2 and purple for O6, upper panel) and residues coordinating the ions (blue, lower panel) are placed on a single protein chain. The 2Fo−Fc electron density around the ligands is contoured at 1 σ (black mesh); the anomalous signal attesting for the presence of Mn2+ ions is contoured at 3 σ (red mesh).

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