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PDBsum entry 5t4x
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Transport protein
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PDB id
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5t4x
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References listed in PDB file
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Key reference
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Title
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Mechanistic insights into the role of prenyl-Binding protein prbp/δ in membrane dissociation of phosphodiesterase 6.
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Authors
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B.M.Qureshi,
A.Schmidt,
E.Behrmann,
J.Bürger,
T.Mielke,
C.M.T.Spahn,
M.Heck,
P.Scheerer.
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Ref.
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Nat Commun, 2018,
9,
90.
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PubMed id
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Abstract
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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.
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