3BDQ
Room Tempreture Crystal Structure of Sterol Carrier Protein-2 Like-2
Summary for 3BDQ
Entry DOI | 10.2210/pdb3bdq/pdb |
Related | 2QZT |
Descriptor | Sterol carrier protein 2-like 2, PALMITIC ACID (3 entities in total) |
Functional Keywords | alpha/beta protein, lipid carrier, sterol carrier protein, lipid transport |
Biological source | Aedes aegypti (yellow fever mosquito) |
Total number of polymer chains | 2 |
Total formula weight | 24016.22 |
Authors | Dyer, D.H.,Lan, Q.,Forest, K.T. (deposition date: 2007-11-15, release date: 2008-01-01, Last modification date: 2024-02-21) |
Primary citation | Dyer, D.H.,Wessely, V.,Forest, K.T.,Lan, Q. Three-dimensional structure/function analysis of SCP-2-like2 reveals differences among SCP-2 family members. J.Lipid Res., 49:644-653, 2008 Cited by PubMed Abstract: Mosquito sterol carrier protein-2 (AeSCP-2) and sterol carrier protein-2-like2 (AeSCP-2L2) are members of the SCP-2 protein family with similar expression profiles in the mosquito life cycle. In an effort to understand how lipids can be transported by different SCP-2 proteins, the three-dimensional crystal structure of AeSCP-2L2 was solved at 1.7 A resolution. AeSCP-2L2 forms a dimer and binds three fatty acids, one of which resides in a position within the internal cavity at a right angle to the others. This first report of ligand-bound dimerized protein in the SCP-2 protein family indicates that the family has a much more divergent mode of interaction with ligands than previously reported. The potential function of AeSCP-2L2 was investigated via in vivo incorporation of [(3)H]cholesterol and [3H]palmitic acid. Overexpression of AeSCP-2L2 in mosquito cells leads to an increased uptake of free fatty acid, whereas knockdown of AeSCP-2L2 in adult females decreases the accumulation of free fatty acid in the fat body from a blood meal. In contrast, overexpression or knockdown of AeSCP-2L2 has no effect on cholesterol uptake. Our results suggest that the main function of AeSCP-2L2 is as a general intracellular fatty acid carrier, as opposed to having a dedicated role in cholesterol transport. PubMed: 18084051DOI: 10.1194/jlr.M700460-JLR200 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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