Sandbox Reserved 344: Difference between revisions
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===Regulatory Domain=== | ===Regulatory Domain=== | ||
The regulatory domain consists of 5 α-helixes and 5 β-sheets. Twofold symmetry is achieved on the α-4 helix, β-5 sheet and α-5 helix face. 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 regulatory domain consists of 5 α-helixes and 5 β-sheets. Twofold symmetry is achieved on the | ||
<scene name='Sandbox_Reserved_344/Dimerization_surface/1'>TextToBeDisplayed</scene> α-4 helix, β-5 sheet and α-5 helix face. 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> | ||