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PDBsum entry 1olm
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Lipid binding protein PDB id
1olm

 

 

 

 

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Contents
Protein chain
395 a.a. *
Ligands
VTQ ×3
Waters ×875
* Residue conservation analysis
PDB id:
1olm
Name: Lipid binding protein
Title: Supernatant protein factor in complex with rrr-alpha- tocopherylquinone: a link between oxidized vitamin e and cholesterol biosynthesis
Structure: Sec14-like protein 2. Chain: a, c. Synonym: supernatant protein factor, alpha-tocopherol associated protein, tap, htap, supernatant protein factor, spf, squalene transfer protein, sec14l2, kiaa1186. Engineered: yes. Sec14-like protein 2. Chain: e. Synonym: supernatant protein factor, alpha-tocopherol associated
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Resolution:
1.95Å     R-factor:   0.181     R-free:   0.211
Authors: A.Stocker,U.Baumann
Key ref:
A.Stocker and U.Baumann (2003). Supernatant protein factor in complex with RRR-alpha-tocopherylquinone: a link between oxidized Vitamin E and cholesterol biosynthesis. J Mol Biol, 332, 759-765. PubMed id: 12972248 DOI: 10.1016/S0022-2836(03)00924-0
Date:
08-Aug-03     Release date:   12-Aug-04    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
O76054  (S14L2_HUMAN) -  SEC14-like protein 2 from Homo sapiens
Seq:
Struc: 		403 a.a.
395 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
DOI no: 10.1016/S0022-2836(03)00924-0 J Mol Biol 332:759-765 (2003)
PubMed id: 12972248  
 
 
Supernatant protein factor in complex with RRR-alpha-tocopherylquinone: a link between oxidized Vitamin E and cholesterol biosynthesis.
A.Stocker, U.Baumann.
 
  ABSTRACT  
 
The vast majority of monomeric lipid transport in nature is performed by lipid-specific protein carriers. This class of proteins can enclose cognate lipid molecules in a hydrophobic cavity and transport them across the aqueous environment. Supernatant protein factor (SPF) is an enigmatic representative of monomeric lipid transporters belonging to the SEC14 family. SPF stimulates squalene epoxidation, a downstream step of the cholesterol biosynthetic pathway, by an unknown mechanism. Here, we present the three-dimensional crystal structure of human SPF in complex with RRR-alpha-tocopherylquinone, the major physiological oxidation product of RRR-alpha-tocopherol, at a resolution of 1.95A. The structure of the complex reveals how SPF sequesters RRR-alpha-tocopherylquinone (RRR-alpha-TQ) in its protein body and permits a comparison with the recently solved structure of human alpha-tocopherol transfer protein (alpha-TTP) in complex with RRR-alpha-tocopherol. Recent findings have shown that RRR-alpha-TQ is reduced in vivo to RRR-alpha-TQH(2), the latter has been suggested to protect low-density lipoprotein (LDL) particles from oxidation. Hence, the antioxidant function of the redox couple RRR-alpha-TQ/RRR-alpha-TQH(2) in blocking LDL oxidation may reduce cellular cholesterol uptake and thus explain how SPF upregulates cholesterol synthesis.
 
  Selected figure(s)  
 
Figure 3.
Figure 3. Stereoview of the SPF-RRR-a-TQ complex in rainbow coloring from blue (N terminus) to red (C terminus) showing the three-helix coil in dark blue, CRAL_TRIO lipid-binding domain in light blue and green, jelly-roll in yellow and red, cavity in gray (for details see Figure 5), lipid-exchange loop in pink and RRR-a-TQ in black. 		Figure 5.
Figure 5. Stereoview of the ligand-binding pockets of: A, SPF with RRR-a-TQ; and B, a-TTP with RRR-a-T. Cavities are shown after least-squares superimposition of the C^a traces of the protein structures. Ligands are shown in black; side-chains in gray; oxygen, nitrogen and sulfur atoms in red, blue and orange, respectively; cavities in light gray. Cavities were calculated with the program VOIDOO.[30.]
 
  The above figures are reprinted by permission from Elsevier: J Mol Biol (2003, 332, 759-765) copyright 2003.  
  Figures were selected by the author.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20230813 K.G.Johnson, and K.Kornfeld (2010).
The CRAL/TRIO and GOLD domain protein TAP-1 regulates RAF-1 activation.
  Dev Biol, 341, 464-471.  
20169582 L.Gille, K.Staniek, T.Rosenau, J.C.Duvigneau, and A.V.Kozlov (2010).
Tocopheryl quinones and mitochondria.
  Mol Nutr Food Res, 54, 601-615.  
19926291 V.A.Bankaitis, C.J.Mousley, and G.Schaaf (2010).
The Sec14 superfamily and mechanisms for crosstalk between lipid metabolism and lipid signaling.
  Trends Biochem Sci, 35, 150-160.  
17543577 F.Schroeder, B.P.Atshaves, A.L.McIntosh, A.M.Gallegos, S.M.Storey, R.D.Parr, J.R.Jefferson, J.M.Ball, and A.B.Kier (2007).
Sterol carrier protein-2: new roles in regulating lipid rafts and signaling.
  Biochim Biophys Acta, 1771, 700-718.  
17439363 M.G.Traber (2007).
Vitamin E regulatory mechanisms.
  Annu Rev Nutr, 27, 347-362.  
17344474 M.M.Ryan, B.R.Temple, S.E.Phillips, and V.A.Bankaitis (2007).
Conformational dynamics of the major yeast phosphatidylinositol transfer protein sec14p: insight into the mechanisms of phospholipid exchange and diseases of sec14p-like protein deficiencies.
  Mol Biol Cell, 18, 1928-1942.  
18060118 V.M.Vecchio, M.Benedetti, D.Migoni, S.A.De Pascali, A.Ciccarese, S.Marsigliante, F.Capitelli, and F.P.Fanizzi (2007).
Highly selective metal mediated ortho-alkylation of phenol. First platinum containing organometallic chromane analogues.
  Dalton Trans, (), 5720-5725.  
17334589 X.Q.Wen, X.J.Li, Z.L.Su, Y.Liu, X.F.Zhou, Y.B.Cai, W.T.Huang, and X.Gao (2007).
Reduced expression of alpha-tocopherol-associated protein is associated with tumor cell proliferation and the increased risk of prostate cancer recurrence.
  Asian J Androl, 9, 206-212.  
16219793 J.L.Goldstein, D.Glossip, S.Nayak, and K.Kornfeld (2006).
The CRAL/TRIO and GOLD domain protein CGR-1 promotes induction of vulval cell fates in Caenorhabditis elegans and interacts genetically with the Ras signaling pathway.
  Genetics, 172, 929-942.  
15580660 C.Schneider (2005).
Chemistry and biology of vitamin E.
  Mol Nutr Food Res, 49, 7.  
15711217 M.G.Traber (2005).
Vitamin E regulation.
  Curr Opin Gastroenterol, 21, 223-227.  
16262698 M.Merkulova, H.Huynh, V.Radchenko, K.Saito, V.Lipkin, T.Shuvaeva, and T.Mustelin (2005).
Secretion of the mammalian Sec14p-like phosphoinositide-binding p45 protein.
  FEBS J, 272, 5595-5605.  
16121400 T.Liu, E.Jenwitheesuk, D.C.Teller, and R.Samudrala (2005).
Structural insights into the cellular retinaldehyde-binding protein (CRALBP).
  Proteins, 61, 412-422.
PDB codes: 1xgg 1xgh
16417456 V.V.Radchenko, M.I.Merkulova, T.M.Shuvaeva, T.N.Simonova, A.A.Bondar, and V.M.Lipkin (2005).
Functional expression and properties of Sec14p-like protein with molecular mass 45 kD from rat olfactory epithelium.
  Biochemistry (Mosc), 70, 1341-1347.  
15753133 A.Stocker (2004).
Molecular mechanisms of vitamin E transport.
  Ann N Y Acad Sci, 1031, 44-59.  
15100222 Z.Wu, A.Hasan, T.Liu, D.C.Teller, and J.W.Crabb (2004).
Identification of CRALBP ligand interactions by photoaffinity labeling, hydrogen/deuterium exchange, and structural modeling.
  J Biol Chem, 279, 27357-27364.  
14657365 K.C.Min, R.A.Kovall, and W.A.Hendrickson (2003).
Crystal structure of human alpha-tocopherol transfer protein bound to its ligand: implications for ataxia with vitamin E deficiency.
  Proc Natl Acad Sci U S A, 100, 14713-14718.
PDB code: 1r5l
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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