Sandbox Reserved 344: Difference between revisions
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<scene name='Sandbox_Reserved_344/Dimerization_surface/1'>α-4 helix, β-5 sheet and α-5 helix face</scene> . The regulatory domain may be phosphorylated at a conserved aspartate by PhoQ, a histidine protein kinase. Phosphorylation of this aspartate stabilizes the homodimer.<ref name = "Bachh2007"/> | <scene name='Sandbox_Reserved_344/Dimerization_surface/1'>α-4 helix, β-5 sheet and α-5 helix face</scene> . The regulatory domain may be phosphorylated at a conserved aspartate by PhoQ, a histidine protein kinase. Phosphorylation of this aspartate stabilizes the homodimer.<ref name = "Bachh2007"/> | ||
The PhoP regulatory domain has intrinsic autophosphatase activity, allowing it to inactivate itself after a delay.<ref name = "Perron-S"> PMID:16339942</ref> | The PhoP regulatory domain has intrinsic autophosphatase activity, allowing it to inactivate itself after a delay.<ref name = "Perron-S"> PMID:16339942</ref> | ||
=====Activated form===== | |||
:Phosphorylation of the regulatory domain stabilizes dimer formation. <ref name = "Bachh2007"/> | |||
:The phosphoryl analog <scene name='Sandbox_Reserved_344/Phosphoryl_analog/1'>Beryllofluoride</scene> BeF<sup>3-</sup> was used during crystalization of the regulatory domain of ''Escherichia coli''. | |||
The Phosphoryl analog made the following bonds: | |||
::F1 to Mg<sup>2+</sup> | |||
::F2 to Thr 79 (Correlated with Ala 80) -> F3? | |||
:: & BBone of Gly 53 | |||
::F3 to Lys 101 (salt bridge) | |||
=====Un-activated form===== | =====Un-activated form===== | ||
:Under normal physiological conditions, unactivated PhoP occurs mainly as a monomer. At higher concentration unactivated PhoP has been shown to dimerize and act similar to activated and dimerized PhoP. Many regulatory domains isolated from members of the OmpR/PhoB family and in their inactive form, crystalize in a form similar to their activated dimers.<ref name = "Bachh2007"/> | :Under normal physiological conditions, unactivated PhoP occurs mainly as a monomer. At higher concentration unactivated PhoP has been shown to dimerize and act similar to activated and dimerized PhoP. Many regulatory domains isolated from members of the OmpR/PhoB family and in their inactive form, crystalize in a form similar to their activated dimers.<ref name = "Bachh2007"/> | ||
===Effector domain=== | ===Effector domain=== | ||