1pz4

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1pz4, resolution 1.35Å

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The structural determination of an insect (mosquito) Sterol Carrier Protein-2 with a ligand bound C16 Fatty Acid at 1.35 A resolution

Overview

Yellow fever mosquito sterol carrier protein (SCP-2) is known to bind to, cholesterol. We report here the three-dimensional structure of the complex, of SCP-2 from Aedes aegypti with a C16 fatty acid to 1.35-A resolution., The protein fold is exceedingly similar to the human and rabbit proteins, which consist of a five-stranded beta-sheet that exhibits strand order, 3-2-1-4-5 with an accompanying layer of four alpha-helices that cover the, beta-sheet. A large cavity exists at the interface of the layer, alpha-helices and the beta-sheet, which serves as the fatty acid binding, site. The carboxylate moiety of the fatty acid is coordinated by a short, loop that connects the first alpha-helix to the first beta-strand, whereas, the acyl chain extends deep into the interior of the protein., Interestingly, the orientation of the fatty acid is opposite to the, observed orientation for Triton X-100 in the SCP-2-like domain from the, peroxisomal multifunctional enzyme (Haapalainen, A. M., van Aalten, D. M., Merilainen, G., Jalonen, J. E., Pirila, P., Wierenga, R. K., Hiltunen, J., K., and Glumoff, T. (2001) J. Mol. Biol. 313, 1127-1138). The present, study suggests that the binding pocket in the SCP-2 family of proteins may, exhibit conformational flexibility to allow coordination of a variety of, lipids.

About this Structure

1PZ4 is a Single protein structure of sequence from Aedes aegypti with PLM as ligand. Full crystallographic information is available from OCA.

Reference

The structural determination of an insect sterol carrier protein-2 with a ligand-bound C16 fatty acid at 1.35-A resolution., Dyer DH, Lovell S, Thoden JB, Holden HM, Rayment I, Lan Q, J Biol Chem. 2003 Oct 3;278(40):39085-91. Epub 2003 Jul 10. PMID:12855689

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