Sandbox Reserved 344: Difference between revisions

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=Introduction=
=Introduction=
PhoP is a cytoplasmic response regulator from the two component system PhoP/PhoQ. This system responds mainly to changes in extracellular Mg2+ concentration and is an important trigger for gram-negative bacteria such as Escherichia coli and Salmonella enterica to become virulent. PhoQ, located across the inner membrane, responds to low Mg2+ concentration by phosphorylating PhoP. Gene regulation and other two component systems respond to the phosphorylated PhoP. Gene regulation is achieved by increased affinity of the homodimer to the PhoP box, a tandem repeat promoter. The response is organism specific but generally involves survival in low Mg2+ environments and virulence. <ref name = "Bachh2007"> PMID:17545283</ref>
PhoP is a cytoplasmic response regulator from the two component system PhoP/PhoQ. This system responds mainly to changes in extracellular Mg<sup>2+</sup> concentration and is an important trigger for gram-negative bacteria such as Escherichia coli and Salmonella enterica to become virulent. PhoQ, located across the inner membrane, responds to low Mg<sup>2+</sup> concentration by phosphorylating PhoP. Gene regulation and other two component systems respond to the phosphorylated PhoP. Gene regulation is achieved by increased affinity of the homodimer to the PhoP box, a tandem repeat promoter. The response is organism specific but generally involves survival in low Mg2+ environments and virulence. <ref name = "Bachh2007"> PMID:17545283</ref>


=Structure=
=Structure=
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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 – 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.
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.
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.


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=====Activated form=====
=====Activated form=====
:Phosphorylation of the regulatory domain stabilizes dimer formation.  
:Phosphorylation of the regulatory domain stabilizes dimer formation.  
:BeF3-: Phosphoryl analog
:BeF<sup>3-</sup>: Phosphoryl analog
:F1 to Mg2+
:F1 to Mg<sup>2+</sup>
:F2 to Thr 79  (Correlated with Ala 80) -> F3?
:F2 to Thr 79  (Correlated with Ala 80) -> F3?
: & BBone of Gly 53
: & BBone of Gly 53
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=Function=
=Function=
Two component systems allow bacteria to respond to changes in their environment. These systems are found mainly in prokaryotes and a few eukaryotes (mack). The PhoP/PhoQ system, found specifically in gram-negative bacteria, react mainly to a drop in extracellular Mg2+. Since the magnesium concentration is typically lower inside the host cell compared to outside, this acts as a trigger to become virulent. Other functions activated by the PhoP/PhoQ system includes adaptation to low Mg2+ conditions, changes in cell wall, expression of proteases to protect against antimicrobial peptides and various other species specific responses. PhoP in Salmonella enterica regulates up to 40 proteins. (Groisman)  
Two component systems allow bacteria to respond to changes in their environment. These systems are found mainly in prokaryotes and a few eukaryotes (mack). The PhoP/PhoQ system, found specifically in gram-negative bacteria, react mainly to a drop in extracellular Mg<sup>2+</sup>. Since the magnesium concentration is typically lower inside the host cell compared to outside, this acts as a trigger to become virulent. Other functions activated by the PhoP/PhoQ system includes adaptation to low Mg<sup>2+</sup> conditions, changes in cell wall, expression of proteases to protect against antimicrobial peptides and various other species specific responses. PhoP in ''Salmonella enterica'' regulates up to 40 proteins. (Groisman)  
PhoP is not limited to direct regulation of gene expression. PhoP may regulate other two component systems at transcription, posttranscription and posttranslation too, in fact PhoP activates the expression of its own phoP gene, resulting in positive feedback and definite conversion to virulence.
PhoP is not limited to direct regulation of gene expression. PhoP may regulate other two component systems at transcription, posttranscription and posttranslation too, in fact PhoP activates the expression of its own phoP gene, resulting in positive feedback and definite conversion to virulence.
The PhoP/PhoQ system may olso be found in non-cytoplasmic pathogens, such as rwinia carotovora supsb. carotovora, a plant pathogen living in the intercellular fluid, or non-pathogenic bacteria (????)
The PhoP/PhoQ system may also be found in non-cytoplasmic pathogens, such as ''Erwinia carotovora supsb. carotovora'', a plant pathogen living in the intercellular fluid, or non-pathogenic bacteria (????)


=Importance of PhoP=
=Importance of PhoP=
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