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原肌球蛋白-肌钙蛋白T共晶体的结构。

Structure of tropomyosin-troponin T cocrystals.

作者信息

Carr H J, O'Brien E J, Morris E P

机构信息

Medical Research Council Cell Biophysics Unit, King's College, London, U.K.

出版信息

J Muscle Res Cell Motil. 1988 Oct;9(5):384-92. doi: 10.1007/BF01774065.

Abstract

Crystals formed from a mixture of tropomyosin and troponin T have an open double-stranded lattice structure with a diamond-shaped repeat. In some regions the appearance in electron micrographs of negatively stained specimens changes from this double-diamond lattice to a more condensed banded crystal form. The double-diamond lattice has plane group symmetry cmm with unit cell 76.3 by 21.7 nm. The molecules form continuous chains along the diagonal of the unit cell and the diagonal length (79.4 nm) is that expected for two tropomyosin molecules joined end-to-end. Computer filtering of the micrographs shows that the strands of the lattice are thicker from the acute vertex of the large diamond to a point about half-way along the side of the diamond, where there is a small blob of density. At the acute vertex of the diamond is a large blob of density which is accentuated, however, by being at the lattice node where strands cross each other, and which is much weaker in regions of the micrographs where the crystals have condensed laterally. The results indicate that troponin T is a long thin molecule running in contact with the tropomyosin strands over 40-50% of the tropomyosin molecular length. The small globular region may represent the end-to-end overlap of tropomyosin but is more likely to be a globular region at the C-terminal region of troponin T.

摘要

由原肌球蛋白和肌钙蛋白T混合物形成的晶体具有开放的双链晶格结构,呈菱形重复排列。在某些区域,负染色标本的电子显微镜图像从这种双菱形晶格变为更致密的带状晶体形式。双菱形晶格具有平面群对称性cmm,晶胞尺寸为76.3×21.7纳米。分子沿着晶胞对角线形成连续链,对角线长度(79.4纳米)是两个首尾相连的原肌球蛋白分子的预期长度。对显微照片进行计算机滤波显示,晶格链从大菱形的锐角顶点到菱形边长约一半处更粗,此处有一个小的密度团块。在菱形的锐角顶点有一个大的密度团块,然而,由于它位于晶格链相互交叉的节点处而显得突出,并且在晶体横向凝聚的显微照片区域中要弱得多。结果表明,肌钙蛋白T是一个细长分子,与原肌球蛋白链接触的长度超过原肌球蛋白分子长度的40 - 50%。这个小的球状区域可能代表原肌球蛋白的首尾重叠部分,但更可能是肌钙蛋白T C末端区域的一个球状区域。

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