Sandbox Reserved 344: Difference between revisions

No edit summary
No edit summary
Line 32: Line 32:


===Effector domain===
===Effector domain===
The effector domain is activated when PhoP is in dimer form. There is no direct change in conformation conferred on the effector domain by the regulatory domain. The PhoP has a winged helix-turn-helix motif characteristic of the OmpR/PhoB family of response regulators.<ref name = "Hickey"> PMID:19652341</ref> This winged helix-turn-helix allows binding to DNA and regulation of transcription. Binding occurs at promoters with two repeats of the sequence (T/G)GTTTA, known as the PhoP box.<ref name = "Groisman"/>
When the regulatory domain is phosphorylated, PhoP forms a homodimer. There is no direct change in conformation conferred on the effector domain by the regulatory domain. It is the dimerization that activates the effector domain.  The PhoP has a winged helix-turn-helix motif characteristic of the OmpR/PhoB family of response regulators.<ref name = "Hickey"> PMID:19652341</ref> This winged helix-turn-helix allows binding to DNA and regulation of transcription. Binding occurs at tandem repeat promoters with two repeats of the sequence (T/G)GTTTA, known as the PhoP box.<ref name = "Groisman"/>


=Function=
=Function=

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA, Rudi Siegling