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Figure 4
AMP-bound and GMP-bound structures. BrabA.11339.a was cocrystallized with AMPPNP and GMPPNP, variants of AMP or GMP that are nonhydrolyzable between the β-­phosphate and γ-phosphate. Left panels, OMIT densities for the AMPPNP (top) and GMPPNP (bottom) cocrystals (see Fig. 3[link] for colors). The σA-weighted 2FoFc electron density for the high-resolution data set is contoured at 1σ (blue) and the corresponding FoFc electron density is contoured at ±3σ (green/red). The right panels show the refined densities for the models refined with AMP (top) and GMP (bottom), respectively. No density is visible beyond the α-phosphate. It is likely that BrabA.11339.a has hydrolyzed the β-phosphate. The nucleotides are bound in the dimer interface and engage in multiple interactions with both protomers.

ISSN: 2053-230X
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