Sandbox Reserved 344: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 14: | Line 14: | ||
===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 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: | The PhoP regulatory domain has intrinsic autophosphatase activity, allowing it to inactivate itself after a delay.<ref name = "Perron-S"> PMID:16339942</ref> | ||
=====Un-activated form===== | =====Un-activated form===== | ||
