Sandbox Reserved 344: Difference between revisions
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: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 | ||
F1 to Mg2+ | :F1 to Mg2+ | ||
F2 to Thr 79 (Correlated with Ala 80) -> F3? | :F2 to Thr 79 (Correlated with Ala 80) -> F3? | ||
: & BBone of Gly 53 | |||
F3 to Lys 101 (salt bridge) | :F3 to Lys 101 (salt bridge) | ||
===Effector domain=== | ===Effector domain=== | ||