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PDBsum entry 5t4x

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protein links
Transport protein PDB id
5t4x

 

 

 

 

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Contents
Protein chain
148 a.a.
Waters ×90
PDB id:
5t4x
Name: Transport protein
Title: Crystal structure of pde6d in apo-state
Structure: Retinal rod rhodopsin-sensitive cgmp 3',5'-cyclic phosphodiesterase subunit delta. Chain: a. Synonym: gmp-pde delta. Engineered: yes
Source: Mus musculus. Mouse. Organism_taxid: 10090. Gene: pde6d. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008
Resolution:
1.81Å     R-factor:   0.184     R-free:   0.214
Authors: B.M.Qureshi,A.Schmidt,P.Scheerer
Key ref: B.M.Qureshi et al. (2018). Mechanistic insights into the role of prenyl-binding protein PrBP/δ in membrane dissociation of phosphodiesterase 6. Nat Commun, 9, 90. PubMed id: 29311697
Date:
30-Aug-16     Release date:   10-Jan-18    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
O55057  (PDE6D_MOUSE) -  Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta from Mus musculus
Seq:
Struc:
150 a.a.
148 a.a.
Key:    PfamA domain  Secondary structure

 Enzyme reactions 
   Enzyme class: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
Nat Commun 9:90 (2018)
PubMed id: 29311697  
 
 
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.
 

 

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