The polyoxometalate W18P2O626–, the Dawson cluster, stabilizes the ribosome sufficiently for the crystallographers to solve the phase problem (1). We have recently been very successful in using data mining to study enzyme interactions with metal ions and in the following work extend this to the polyoxometalate system (2). In the following we characterize the interaction of the Dawson cluster with the ribosome by investigating the nature of the interactions that are found to stabilize the polyoxometalate-ribosome structure. A range of different systems are found demonstrating a variety of different interactions with the ribosome including two Dawson units that are very close to each other, herein referred to as the Double Dawson structure. Although well-documented that bridging oxygen atoms are the main basic sites on other polyoxometalates the W=O groups are the main sites of the polyoxometalate interacting with the ribosome. Furthermore, the peptide chain backbone on the ribosome hosts constitutes the main sites that associate with the Double Dawson structure. We conclude that the Double Dawson structure on the ribosome is a real structure because it is geometrically competent and in line with other Double Dawson clusters previously observed in the solid state and solution.

Double dawson cluster on the ribosome

2019 Spring National Meeting

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