Fig. 1: Structure of the nuclease domain of EsaD and EsaDc-EsaG complex. | Nature Communications

Fig. 1: Structure of the nuclease domain of EsaD and EsaDc-EsaG complex.

From: A toxin-deformation dependent inhibition mechanism in the T7SS toxin-antitoxin system of Gram-positive bacteria

Fig. 1

a Domain architecture of EsaD and EsaG, with individual domains colored differently. Similar color schemes are used in the other figures unless otherwise indicated. b Crystal structure of EsaG. The α-helices and β-strands are labeled from A’ to E’ and from 1’ to 4’, respectively. c Crystal structure of the nuclease domain of EsaD. The α-helices and β-strands are labeled from A to B and from 1 to 8, respectively. The magnesium ion (green sphere) is coordinated to an oxygen atom of N551 and five waters (red spheres). d Crystal structure of EsaDc-EsaG complex in one asymmetric unit. The NF binding site (e) and CF binding site (f) on EsaG are shown in the expanded view.

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