PhoP-PhoQ: Difference between revisions

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In this structure, Beryllofluoride (BeF<sub>3</sub><sup>-</sup>) is used as a phosphoryl analog to induce the active state conformation. There are numerous bonds that form as a result of BeF<sub>3</sub><sup>-</sup> coordination. F<sub>1</sub> of BeF<sub>3</sub><sup>-</sup> helps satisfy the octahedral coordination of a present active site Mg<sup>2+</sup>. The conserved active site lysine, Lys101, forms important intramolecular and intermolecular salt bridges, one of which is with F<sub>3</sub> of BeF<sub>3</sub><sup>-</sup>. Finally, a conserved "switch residue" Thr79, involved in the activation of all response regulators, forms a H-bond with F<sub>2</sub> of BeF<sub>3</sub><sup>-</sup>.
In this structure, <scene name='Sandbox_Reserved_344/P-analog/1'>Beryllofluoride</scene> (BeF<sub>3</sub><sup>-</sup>) is used as a phosphoryl analog to induce the active state conformation. There are numerous bonds that form as a result of BeF<sub>3</sub><sup>-</sup> coordination. F<sub>1</sub> of BeF<sub>3</sub><sup>-</sup> helps satisfy the octahedral coordination of a present active site Mg<sup>2+</sup>. The conserved active site lysine, Lys101, forms important intramolecular and intermolecular salt bridges, one of which is with F<sub>3</sub> of BeF<sub>3</sub><sup>-</sup>. A conserved "switch residue" Thr79, involved in the activation of all response regulators, forms a H-bond with F<sub>2</sub> of BeF<sub>3</sub><sup>-</sup>. F<sub>2</sub> of BeF<sub>3</sub><sup>-</sup> also forms a H-bond with the backbone nitrogen atom of Gly53.
</StructureSection>
</StructureSection>
===PhoP-PhoQ and Virulence===
===PhoP-PhoQ and Virulence===

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Michal Harel, Andrew Brockfield, Alexander Berchansky