1PZ4
The structural determination of an insect (mosquito) Sterol Carrier Protein-2 with a ligand bound C16 Fatty Acid at 1.35 A resolution
1PZ4 の概要
エントリーDOI | 10.2210/pdb1pz4/pdb |
分子名称 | sterol carrier protein 2, PALMITIC ACID (3 entities in total) |
機能のキーワード | alpha and beta, lipid binding protein |
由来する生物種 | Aedes aegypti (yellow fever mosquito) |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 13112.30 |
構造登録者 | Dyer, D.H.,Lovell, S.,Thoden, J.B.,Holden, H.M.,Rayment, I.,Lan, Q. (登録日: 2003-07-09, 公開日: 2003-09-30, 最終更新日: 2024-02-14) |
主引用文献 | Dyer, D.H.,Lovell, S.,Thoden, J.B.,Holden, H.M.,Rayment, I.,Lan, Q. The Structural Determination of an Insect Sterol Carrier Protein-2 with a Ligand-bound C16 Fatty Acid at 1.35A Resolution J.Biol.Chem., 278:39085-39091, 2003 Cited by PubMed Abstract: 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. PubMed: 12855689DOI: 10.1074/jbc.M306214200 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.35 Å) |
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