 |
PDBsum entry 5t4x
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
|
|
|
|
|
|
|
Transport protein
|
PDB id
|
|
|
|
5t4x
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
| |
|
|
Nat Commun
9:90
(2018)
|
|
PubMed id:
|
|
|
|
|
| |
|
Mechanistic insights into the role of prenyl-binding protein PrBP/δ in membrane dissociation of phosphodiesterase 6.
|
|
B.M.Qureshi,
A.Schmidt,
E.Behrmann,
J.Bürger,
T.Mielke,
C.M.T.Spahn,
M.Heck,
P.Scheerer.
|
|
|
|
| |
ABSTRACT
|
|
|
| |
|
Isoprenylated proteins are associated with membranes and their
inter-compartmental distribution is regulated by solubilization factors, which
incorporate lipid moieties in hydrophobic cavities and thereby facilitate
free diffusion during trafficking. Here we report the crystal structure of a
solubilization factor, the prenyl-binding protein (PrBP/δ), at 1.81 Å
resolution in its ligand-free apo-form. Apo-PrBP/δ harbors a preshaped, deep
hydrophobic cavity, capacitating apo-PrBP/δ to readily bind its prenylated
cargo. To investigate the molecular mechanism of cargo solubilization we
analyzed the PrBP/δ-induced membrane dissociation of rod photoreceptor
phosphodiesterase (PDE6). The results suggest that PrBP/δ exclusively interacts
with the soluble fraction of PDE6. Depletion of soluble species in turn leads to
dissociation of membrane-bound PDE6, as both are in equilibrium. This
"solubilization by depletion" mechanism of PrBP/δ differs from the
extraction of prenylated proteins by the similar folded solubilization factor
RhoGDI, which interacts with membrane bound cargo via an N-terminal structural
element lacking in PrBP/δ.
|
|
|
|
|
|
|
 |
 |
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
');
}
}
 |