Source 1primary paper2017Biochemistry
Toolkit/RhoPDE C-terminal phosphodiesterase catalytic domain
RhoPDE C-terminal phosphodiesterase catalytic domain
Also known as: isolated PDE domain, phosphodiesterase domain
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The RhoPDE C-terminal phosphodiesterase catalytic domain is the isolated catalytic region of the rhodopsin/phosphodiesterase fusion protein RhoPDE from the choanoflagellate Salpingoeca rosetta. It has been expressed, purified, and structurally characterized by crystallography, while the parent full-length protein was reported to function as a cGMP-selective phosphodiesterase.
Usefulness & Problems
Why this is useful
This domain is useful as a structurally defined phosphodiesterase module from a rhodopsin-linked enzyme with reported optogenetic relevance in its full-length context. It provides a tractable system for studying the catalytic region of RhoPDE and for investigating cyclic nucleotide hydrolysis properties associated with the parent enzyme.
Source:
RhoPDE has potential as an optogenetic tool catalyzing the hydrolysis of cyclic nucleotides.
Problem solved
It helps address the need for an isolated, purifiable catalytic domain from RhoPDE for biochemical and structural analysis. The available evidence supports its use in dissecting the phosphodiesterase portion of a rhodopsin-PDE fusion protein from Salpingoeca rosetta.
Source:
RhoPDE has potential as an optogenetic tool catalyzing the hydrolysis of cyclic nucleotides.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Mechanisms
HeterodimerizationTechniques
Structural CharacterizationTarget processes
No target processes tagged yet.
Implementation Constraints
The source literature reports an expression and purification system for RhoPDE and a crystal structure of the C-terminal phosphodiesterase catalytic domain. No additional implementation details such as cofactors, host system, delivery strategy, or construct boundaries are provided in the supplied evidence.
Evidence for this specific isolated domain is limited mainly to expression, purification, and crystallographic characterization. Reported lack of light modulation applies to RhoPDE phosphodiesterase activity in the source study, and no independent evidence here demonstrates light control, cellular performance, or standalone functional validation of the isolated domain.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
RhoPDE has potential as an optogenetic tool for catalyzing hydrolysis of cyclic nucleotides.
RhoPDE has potential as an optogenetic tool catalyzing the hydrolysis of cyclic nucleotides.
RhoPDE has potential as an optogenetic tool for catalyzing hydrolysis of cyclic nucleotides.
RhoPDE has potential as an optogenetic tool catalyzing the hydrolysis of cyclic nucleotides.
RhoPDE has potential as an optogenetic tool for catalyzing hydrolysis of cyclic nucleotides.
RhoPDE has potential as an optogenetic tool catalyzing the hydrolysis of cyclic nucleotides.
RhoPDE has potential as an optogenetic tool for catalyzing hydrolysis of cyclic nucleotides.
RhoPDE has potential as an optogenetic tool catalyzing the hydrolysis of cyclic nucleotides.
RhoPDE has potential as an optogenetic tool for catalyzing hydrolysis of cyclic nucleotides.
RhoPDE has potential as an optogenetic tool catalyzing the hydrolysis of cyclic nucleotides.
RhoPDE has potential as an optogenetic tool for catalyzing hydrolysis of cyclic nucleotides.
RhoPDE has potential as an optogenetic tool catalyzing the hydrolysis of cyclic nucleotides.
RhoPDE has potential as an optogenetic tool for catalyzing hydrolysis of cyclic nucleotides.
RhoPDE has potential as an optogenetic tool catalyzing the hydrolysis of cyclic nucleotides.
RhoPDE acts as a cGMP-selective phosphodiesterase.
The protein acts as a cGMP-selective phosphodiesterase.
RhoPDE acts as a cGMP-selective phosphodiesterase.
The protein acts as a cGMP-selective phosphodiesterase.
RhoPDE acts as a cGMP-selective phosphodiesterase.
The protein acts as a cGMP-selective phosphodiesterase.
RhoPDE acts as a cGMP-selective phosphodiesterase.
The protein acts as a cGMP-selective phosphodiesterase.
RhoPDE acts as a cGMP-selective phosphodiesterase.
The protein acts as a cGMP-selective phosphodiesterase.
RhoPDE acts as a cGMP-selective phosphodiesterase.
The protein acts as a cGMP-selective phosphodiesterase.
RhoPDE acts as a cGMP-selective phosphodiesterase.
The protein acts as a cGMP-selective phosphodiesterase.
RhoPDE phosphodiesterase activity does not appear to be modulated by light.
However, the activity does not appear to be modulated by light.
RhoPDE phosphodiesterase activity does not appear to be modulated by light.
However, the activity does not appear to be modulated by light.
RhoPDE phosphodiesterase activity does not appear to be modulated by light.
However, the activity does not appear to be modulated by light.
RhoPDE phosphodiesterase activity does not appear to be modulated by light.
However, the activity does not appear to be modulated by light.
RhoPDE phosphodiesterase activity does not appear to be modulated by light.
However, the activity does not appear to be modulated by light.
RhoPDE phosphodiesterase activity does not appear to be modulated by light.
However, the activity does not appear to be modulated by light.
RhoPDE phosphodiesterase activity does not appear to be modulated by light.
However, the activity does not appear to be modulated by light.
This study provides an expression and purification system for RhoPDE.
Here we provide an expression and purification system for RhoPDE
This study provides an expression and purification system for RhoPDE.
Here we provide an expression and purification system for RhoPDE
This study provides an expression and purification system for RhoPDE.
Here we provide an expression and purification system for RhoPDE
This study provides an expression and purification system for RhoPDE.
Here we provide an expression and purification system for RhoPDE
This study provides an expression and purification system for RhoPDE.
Here we provide an expression and purification system for RhoPDE
This study provides an expression and purification system for RhoPDE.
Here we provide an expression and purification system for RhoPDE
This study provides an expression and purification system for RhoPDE.
Here we provide an expression and purification system for RhoPDE
RhoPDE is a type I rhodopsin/phosphodiesterase fusion protein from Salpingoeca rosetta.
RhoPDE is a type I rhodopsin/phosphodiesterase gene fusion product from the choanoflagellate Salpingoeca rosetta.
RhoPDE is a type I rhodopsin/phosphodiesterase fusion protein from Salpingoeca rosetta.
RhoPDE is a type I rhodopsin/phosphodiesterase gene fusion product from the choanoflagellate Salpingoeca rosetta.
RhoPDE is a type I rhodopsin/phosphodiesterase fusion protein from Salpingoeca rosetta.
RhoPDE is a type I rhodopsin/phosphodiesterase gene fusion product from the choanoflagellate Salpingoeca rosetta.
RhoPDE is a type I rhodopsin/phosphodiesterase fusion protein from Salpingoeca rosetta.
RhoPDE is a type I rhodopsin/phosphodiesterase gene fusion product from the choanoflagellate Salpingoeca rosetta.
RhoPDE is a type I rhodopsin/phosphodiesterase fusion protein from Salpingoeca rosetta.
RhoPDE is a type I rhodopsin/phosphodiesterase gene fusion product from the choanoflagellate Salpingoeca rosetta.
RhoPDE is a type I rhodopsin/phosphodiesterase fusion protein from Salpingoeca rosetta.
RhoPDE is a type I rhodopsin/phosphodiesterase gene fusion product from the choanoflagellate Salpingoeca rosetta.
RhoPDE is a type I rhodopsin/phosphodiesterase fusion protein from Salpingoeca rosetta.
RhoPDE is a type I rhodopsin/phosphodiesterase gene fusion product from the choanoflagellate Salpingoeca rosetta.
Purified RhoPDE has an absorption maximum at 490 nm in the dark state and shifts to 380 nm upon light exposure.
The purified protein exhibits an absorption maximum at 490 nm in the dark state, which shifts to 380 nm upon exposure to light.
absorption maximum 490 nmabsorption maximum 380 nm
Purified RhoPDE has an absorption maximum at 490 nm in the dark state and shifts to 380 nm upon light exposure.
The purified protein exhibits an absorption maximum at 490 nm in the dark state, which shifts to 380 nm upon exposure to light.
absorption maximum 490 nmabsorption maximum 380 nm
Purified RhoPDE has an absorption maximum at 490 nm in the dark state and shifts to 380 nm upon light exposure.
The purified protein exhibits an absorption maximum at 490 nm in the dark state, which shifts to 380 nm upon exposure to light.
absorption maximum 490 nmabsorption maximum 380 nm
Purified RhoPDE has an absorption maximum at 490 nm in the dark state and shifts to 380 nm upon light exposure.
The purified protein exhibits an absorption maximum at 490 nm in the dark state, which shifts to 380 nm upon exposure to light.
absorption maximum 490 nmabsorption maximum 380 nm
Purified RhoPDE has an absorption maximum at 490 nm in the dark state and shifts to 380 nm upon light exposure.
The purified protein exhibits an absorption maximum at 490 nm in the dark state, which shifts to 380 nm upon exposure to light.
absorption maximum 490 nmabsorption maximum 380 nm
Purified RhoPDE has an absorption maximum at 490 nm in the dark state and shifts to 380 nm upon light exposure.
The purified protein exhibits an absorption maximum at 490 nm in the dark state, which shifts to 380 nm upon exposure to light.
absorption maximum 490 nmabsorption maximum 380 nm
Purified RhoPDE has an absorption maximum at 490 nm in the dark state and shifts to 380 nm upon light exposure.
The purified protein exhibits an absorption maximum at 490 nm in the dark state, which shifts to 380 nm upon exposure to light.
absorption maximum 490 nmabsorption maximum 380 nm
The isolated RhoPDE phosphodiesterase domain forms a dimer similar to human PDE9 in the X-ray structure.
The isolated PDE domain was crystallized, and the X-ray structure showed the protein to be a dimer similar to human PDE9.
The isolated RhoPDE phosphodiesterase domain forms a dimer similar to human PDE9 in the X-ray structure.
The isolated PDE domain was crystallized, and the X-ray structure showed the protein to be a dimer similar to human PDE9.
The isolated RhoPDE phosphodiesterase domain forms a dimer similar to human PDE9 in the X-ray structure.
The isolated PDE domain was crystallized, and the X-ray structure showed the protein to be a dimer similar to human PDE9.
The isolated RhoPDE phosphodiesterase domain forms a dimer similar to human PDE9 in the X-ray structure.
The isolated PDE domain was crystallized, and the X-ray structure showed the protein to be a dimer similar to human PDE9.
The isolated RhoPDE phosphodiesterase domain forms a dimer similar to human PDE9 in the X-ray structure.
The isolated PDE domain was crystallized, and the X-ray structure showed the protein to be a dimer similar to human PDE9.
The isolated RhoPDE phosphodiesterase domain forms a dimer similar to human PDE9 in the X-ray structure.
The isolated PDE domain was crystallized, and the X-ray structure showed the protein to be a dimer similar to human PDE9.
The isolated RhoPDE phosphodiesterase domain forms a dimer similar to human PDE9 in the X-ray structure.
The isolated PDE domain was crystallized, and the X-ray structure showed the protein to be a dimer similar to human PDE9.
RhoPDE is active with cAMP as a substrate, with a roughly 5-7-fold lower kcat than for cGMP.
The protein is also active with cAMP as a substrate, but with a roughly 5-7-fold lower kcat.
kcat fold difference 5-7-fold lower
RhoPDE is active with cAMP as a substrate, with a roughly 5-7-fold lower kcat than for cGMP.
The protein is also active with cAMP as a substrate, but with a roughly 5-7-fold lower kcat.
kcat fold difference 5-7-fold lower
RhoPDE is active with cAMP as a substrate, with a roughly 5-7-fold lower kcat than for cGMP.
The protein is also active with cAMP as a substrate, but with a roughly 5-7-fold lower kcat.
kcat fold difference 5-7-fold lower
RhoPDE is active with cAMP as a substrate, with a roughly 5-7-fold lower kcat than for cGMP.
The protein is also active with cAMP as a substrate, but with a roughly 5-7-fold lower kcat.
kcat fold difference 5-7-fold lower
RhoPDE is active with cAMP as a substrate, with a roughly 5-7-fold lower kcat than for cGMP.
The protein is also active with cAMP as a substrate, but with a roughly 5-7-fold lower kcat.
kcat fold difference 5-7-fold lower
RhoPDE is active with cAMP as a substrate, with a roughly 5-7-fold lower kcat than for cGMP.
The protein is also active with cAMP as a substrate, but with a roughly 5-7-fold lower kcat.
kcat fold difference 5-7-fold lower
RhoPDE is active with cAMP as a substrate, with a roughly 5-7-fold lower kcat than for cGMP.
The protein is also active with cAMP as a substrate, but with a roughly 5-7-fold lower kcat.
kcat fold difference 5-7-fold lower
RhoPDE contains an even number of transmembrane segments with both N- and C-termini on the cytoplasmic surface.
We show that RhoPDE contains an even number of transmembrane segments, with N- and C-termini both located on the cytoplasmic surface of the cell membrane.
RhoPDE contains an even number of transmembrane segments with both N- and C-termini on the cytoplasmic surface.
We show that RhoPDE contains an even number of transmembrane segments, with N- and C-termini both located on the cytoplasmic surface of the cell membrane.
RhoPDE contains an even number of transmembrane segments with both N- and C-termini on the cytoplasmic surface.
We show that RhoPDE contains an even number of transmembrane segments, with N- and C-termini both located on the cytoplasmic surface of the cell membrane.
RhoPDE contains an even number of transmembrane segments with both N- and C-termini on the cytoplasmic surface.
We show that RhoPDE contains an even number of transmembrane segments, with N- and C-termini both located on the cytoplasmic surface of the cell membrane.
RhoPDE contains an even number of transmembrane segments with both N- and C-termini on the cytoplasmic surface.
We show that RhoPDE contains an even number of transmembrane segments, with N- and C-termini both located on the cytoplasmic surface of the cell membrane.
RhoPDE contains an even number of transmembrane segments with both N- and C-termini on the cytoplasmic surface.
We show that RhoPDE contains an even number of transmembrane segments, with N- and C-termini both located on the cytoplasmic surface of the cell membrane.
RhoPDE contains an even number of transmembrane segments with both N- and C-termini on the cytoplasmic surface.
We show that RhoPDE contains an even number of transmembrane segments, with N- and C-termini both located on the cytoplasmic surface of the cell membrane.
The isolated RhoPDE phosphodiesterase domain is active, but its cGMP kcat is roughly 6-9-fold lower than that of full-length RhoPDE.
A truncation consisting solely of the phosphodiesterase domain is also active with a kcat for cGMP roughly 6-9-fold lower than that of the full-length protein.
kcat fold difference 6-9-fold lower
The isolated RhoPDE phosphodiesterase domain is active, but its cGMP kcat is roughly 6-9-fold lower than that of full-length RhoPDE.
A truncation consisting solely of the phosphodiesterase domain is also active with a kcat for cGMP roughly 6-9-fold lower than that of the full-length protein.
kcat fold difference 6-9-fold lower
The isolated RhoPDE phosphodiesterase domain is active, but its cGMP kcat is roughly 6-9-fold lower than that of full-length RhoPDE.
A truncation consisting solely of the phosphodiesterase domain is also active with a kcat for cGMP roughly 6-9-fold lower than that of the full-length protein.
kcat fold difference 6-9-fold lower
The isolated RhoPDE phosphodiesterase domain is active, but its cGMP kcat is roughly 6-9-fold lower than that of full-length RhoPDE.
A truncation consisting solely of the phosphodiesterase domain is also active with a kcat for cGMP roughly 6-9-fold lower than that of the full-length protein.
kcat fold difference 6-9-fold lower
The isolated RhoPDE phosphodiesterase domain is active, but its cGMP kcat is roughly 6-9-fold lower than that of full-length RhoPDE.
A truncation consisting solely of the phosphodiesterase domain is also active with a kcat for cGMP roughly 6-9-fold lower than that of the full-length protein.
kcat fold difference 6-9-fold lower
The isolated RhoPDE phosphodiesterase domain is active, but its cGMP kcat is roughly 6-9-fold lower than that of full-length RhoPDE.
A truncation consisting solely of the phosphodiesterase domain is also active with a kcat for cGMP roughly 6-9-fold lower than that of the full-length protein.
kcat fold difference 6-9-fold lower
The isolated RhoPDE phosphodiesterase domain is active, but its cGMP kcat is roughly 6-9-fold lower than that of full-length RhoPDE.
A truncation consisting solely of the phosphodiesterase domain is also active with a kcat for cGMP roughly 6-9-fold lower than that of the full-length protein.
kcat fold difference 6-9-fold lower
Approval Evidence
1 source2 linked approval claimsfirst-pass slug rhopde-c-terminal-phosphodiesterase-catalytic-domain
Here we provide an expression and purification system for RhoPDE, as well as a crystal structure of the C-terminal phosphodiesterase catalytic domain.
Source:
structuresupports
The isolated RhoPDE phosphodiesterase domain forms a dimer similar to human PDE9 in the X-ray structure.
The isolated PDE domain was crystallized, and the X-ray structure showed the protein to be a dimer similar to human PDE9.
Source:
truncation activitysupports
The isolated RhoPDE phosphodiesterase domain is active, but its cGMP kcat is roughly 6-9-fold lower than that of full-length RhoPDE.
A truncation consisting solely of the phosphodiesterase domain is also active with a kcat for cGMP roughly 6-9-fold lower than that of the full-length protein.
Source:
Comparisons
Source-backed strengths
The domain has direct structural support from a crystal structure and is associated with an expression and purification system reported in the source study. The parent RhoPDE protein was characterized as a cGMP-selective phosphodiesterase, supporting relevance of this catalytic region to cyclic nucleotide hydrolysis.
Ranked Citations
- 1.