分辨率为2.8埃的泛素三维结构。
Three-dimensional structure of ubiquitin at 2.8 A resolution.
作者信息
Vijay-Kumar S, Bugg C E, Wilkinson K D, Cook W J
出版信息
Proc Natl Acad Sci U S A. 1985 Jun;82(11):3582-5. doi: 10.1073/pnas.82.11.3582.
Abstract
The three-dimensional structure of ubiquitin has been determined at 2.8 A resolution. X-ray diffraction data for the native protein and derivatives were collected with an automated diffractometer. Phases were obtained by use of a single isomorphous mercuric acetate derivative. The molecule contains a pronounced hydrophobic core. Prominent secondary structural features include three and one-half turns of alpha-helix, a mixed beta-sheet that contains four strands, and seven reverse turns. The histidine, tyrosine, and two phenylalanine residues are located on the surface of the molecule.
摘要
泛素的三维结构已在2.8埃分辨率下确定。天然蛋白质及其衍生物的X射线衍射数据是用自动衍射仪收集的。通过使用单一的同晶型醋酸汞衍生物获得了相位。该分子含有一个明显的疏水核心。突出的二级结构特征包括三个半圈的α螺旋、一个包含四条链的混合β折叠片以及七个反向转角。组氨酸、酪氨酸和两个苯丙氨酸残基位于分子表面。
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