3-DIMENSIONAL STRUCTURE IN SOLUTION OF A WHEAT LIPID-TRANSFER PROTEIN FROM MULTIDIMENSIONAL H-1-NMR DATA - A NEW FOLDING FOR LIPID CARRIERS
3-DIMENSIONAL STRUCTURE IN SOLUTION OF A WHEAT LIPID-TRANSFER PROTEIN FROM MULTIDIMENSIONAL H-1-NMR DATA - A NEW FOLDING FOR LIPID CARRIERS
复制标题
DOI：
10.1111/j.1432-1033.1994.tb20066.x
复制
发表时间：
1994-12-01
期刊：
影响因子：
--
通讯作者：
VOVELLE, F
中科院分区：
文献类型：
--
作者：
GINCEL, E;SIMORRE, JP;VOVELLE, F
二维和三维1H-1-NMR实验数据[Simorre，J. P.，Caille，A.，马里恩，D.，Marion，D.和Ptak，M.（1991）Biochemistry 30，11600-11608]通过使用距离几何学、模拟退火、能量最小化和分子动力学技术来构建非特异性小麦脂质转移蛋白（LTP）的三维结构的模型。使用从NOE交叉峰强度导出的第一组881个距离约束来生成74个初始结构。通过考虑螺旋二级结构组织和空间要求，消除了蛋白质结构的一族拓扑镜像。NOE强度的反向计算使我们引入了535个额外的距离约束。最后，选择21个结构作为蛋白质结构的代表。多肽骨架折叠成简单且原始的右旋缠绕。它由一束由柔性环连接的四个螺旋组成，该柔性环紧靠C末端片段包装，形成非标准的萨克斯管样形状。折叠的蛋白质通过疏水相互作用和蛋白质每一侧成对结合的四个二硫键来稳定。位于蛋白质后半部分的残基形成的疏水裂缝可能是脂质结合的潜在位点。
Two-dimensional and three-dimensional H-1-NMR experimental data [Simorre, J. P., Caille, A., Marion, D., Marion, D. and Ptak, M. (1991) Biochemistry 30, 11600-11608] were used to build models of the three-dimensional structure of a non-specific wheat lipid-transfer protein (LTP) by using distance geometry, simulated annealing, energy minimization and molecular dynamics techniques. A first set of 881 distance constraints derived from NOE cross-peak intensities was used to generate 74 initial structures. One family of topological mirror images of the protein structure was eliminated by considering helical secondary-structure organization and steric requirements. Back calculations of NOE intensities led us to introduce 535 additional distance constraints. Finally, 21 structures were selected as representative of the structure of the protein. The polypeptide backbone folds into a simple and original right-handed winding. It is composed of a bundle of four helices linked by flexible loops, which is packed against a C-terminal fragment forming a non-standard saxophone-like shape. The folded protein is stabilized by hydrophobic interactions and the four disulfide bridges combined by pairs on each side of the protein. An hydrophobic cleft, formed by residues located in the second half of the protein could be a potential site for the binding of lipids.