2NBM

Solution NMR structure of ligand free sterol carrier protein 2 like 2 from Aedes aegypti

2NBM の概要

• エントリーDOI: 10.2210/pdb2nbm/pdb
• NMR情報: BMRB: 25983
• 分子名称: Sterol carrier protein 2-like 2 (1 entity in total)
• 機能のキーワード: scp2l2, aedes aegypti, lipid transport
• 由来する生物種: Aedes aegypti (Yellowfever mosquito)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11940.76

構造登録者

Singarapu, K.K.,Ummanni, R. (登録日: 2016-03-07, 公開日: 2017-03-08, 最終更新日: 2024-05-15)

主引用文献

Singarapu, K.K.,Ahuja, A.,Potula, P.R.,Ummanni, R.
Solution Nuclear Magnetic Resonance Studies of Sterol Carrier Protein 2 Like 2 (SCP2L2) Reveal the Insecticide Specific Structural Characteristics of SCP2 Proteins in Aedes aegypti Mosquitoes
Biochemistry, 55:4919-4927, 2016

PubMed Abstract: Sterol carrier protein 2 like 2 from Aedes aegypti (AeSCP2L2) plays an important role in lipid transport in mosquitoes for its routine metabolic processes. Repeated unsuccessful attempts to crystallize ligand free SCP2L2 prompted us to undertake nuclear magnetic resonance (NMR) spectroscopy to determine its three-dimensional structure. We report here the three-dimensional structures and dynamics of apo-AeSCP2L2 and its complex with palmitate. The (15)N heteronuclear single-quantum coherence spectrum of apo-AeSCP2L2 displayed multiple peaks for some of the amide resonances, implying the presence of multiple conformations in solution, which are transformed to a single conformation upon formation of the complex with plamitate. The three-dimensional structures of apo-AeSCP2L2 and palmitated AeSCP2L2 reveal an α/β mixed fold, with five β-strands and four α-helices, very similar to the other SCP2 protein structures. Unlike the crystal structure of palmitated AeSCP2L2, both solution structures are monomeric. It is further confirmed by the rotational correlation times determined by NMR relaxation times (T1 and T2) of the amide protons. In addition, the palmitated AeSCP2L2 structure contains two palmitate ligands, bound in the binding pocket, unlike the three palmitates bound in the dimeric form of AeSCP2L2 in the crystals. The relaxation experiments revealed that complex formation significantly reduces the dynamics of the protein in solution.

PubMed: 27508310
DOI: 10.1021/acs.biochem.6b00322

実験手法

SOLUTION NMR