Sandbox Reserved 344: Difference between revisions
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The PhoP regulatory domain has intrinsic autophosphatase activity, allowing it to inactivate itself after a delay. | The PhoP regulatory domain has intrinsic autophosphatase activity, allowing it to inactivate itself after a delay. | ||
=====: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 in a similar way 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. | :Under normal physiological conditions, unactivated PhoP occurs mainly as a monomer. At higher concentration unactivated PhoP has been shown to dimerize and act in a similar way 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. | ||
=====:Activated form===== | |||
:Phosphorylation of the regulatory domain stabilizes dimer formation. | :Phosphorylation of the regulatory domain stabilizes dimer formation. | ||
BeF3-: Phosphoryl analog | BeF3-: Phosphoryl analog | ||