Streptococcal M protein: alpha-helical coiled-coil structure and arrangement on the cell surface.

机译：链球菌M蛋白：α-螺旋卷曲螺旋结构及其在细胞表面的排列。

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The conformation and molecular dimensions of purified type 6 streptococcal M proteins establish the close structural relationship of these molecules to tropomyosin. Ultracentrifuge studies reveal that the M molecules exist as stable dimers; circular dichroism spectra indicate that the molecules contain about 70% alpha helix; and fiber x-ray diffraction diagrams show the characteristic reflections of the alpha-helical pattern. Electron microscopic images of M protein shadowed with platinum reveal rod-shaped molecules having the same width as tropomyosin. However, the lengths of the M molecules are about 30% shorter than lengths predicted by assuming a completely alpha-helical molecule. These findings indicate that the structure of the M6 protein is primarily alpha-helical coiled coil. Comparison of the lengths of the fibers on the surface of the streptococcus and the isolated M proteins suggests that each fiber on the cell wall consists of a single M-protein molecule approximately 500 A long. The structure determined for these fimbriae is the first alpha-helical coiled-coil conformation to be demonstrated for bacterial surface projections.

机译：纯化的6型链球菌M蛋白的构象和分子尺寸建立了这些分子与原肌球蛋白的紧密结构关系。超速离心研究表明，M分子以稳定的二聚体形式存在。圆二色性光谱表明该分子包含约70％的α螺旋；纤维X射线衍射图显示了α螺旋图案的特征反射。涂有铂的M蛋白的电子显微镜图像显示出棒状分子，其宽度与原肌球蛋白相同。但是，M分子的长度比假定完全为α螺旋的分子所预测的长度短约30％。这些发现表明，M6蛋白的结构主要是α-螺旋卷曲螺旋。比较链球菌和分离出的M蛋白表面的纤维长度，表明细胞壁上的每根纤维都由一个大约500 A长的M蛋白分子组成。为这些菌毛确定的结构是细菌表面投影所证明的第一个α-螺旋卷曲螺旋构象。

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期刊名称 Proceedings of the National Academy of Sciences of the United States of America
作者
G N Phillips Jr; P F Flicker; C Cohen; B N Manjula; V A Fischetti;
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年(卷),期 1981(78),8
年度 1981
页码 4689–4693
总页数 5
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专利

1. Coiled-coil structure of group A streptococcal M proteins. Different temperature stability of class A and C proteins by hydrophobic-nonhydrophobic amino acid substitutions at heptad positions a and d. [J] . Cedervall T, Johansson MU, Akerstrom B Biochemistry . 1997,第16期

机译：A组链球菌M蛋白的螺旋结构。 A和C类蛋白在七肽位a和d处的疏水-非疏水氨基酸取代具有不同的温度稳定性。
2. The C-terminal portion of the fibrinogen-binding protein of Streptococcus equi subsp equi contains extensive alpha-helical coiled-coil structure and contributes to thermal stability [J] . Meehan M., Kelly SM., Price NC., FEMS Microbiology Letters . 2002,第1期

机译：马链球菌马亚种的血纤蛋白原结合蛋白的C端部分含有大量的α螺旋卷曲螺旋结构，并有助于热稳定性
3. THE C-TERMINAL DOMAIN OF CARTILAGE MATRIX PROTEIN ASSEMBLES INTO A TRIPLE-STRANDED ALPHA-HELICAL COILED-COIL STRUCTURE [J] . Beck K., Bohan CA., Bachinger HP., Journal of Molecular Biology . 1996,第5期

机译：到三链α-螺旋盘绕结构的软骨基质蛋白组件的C末端域
4. The role of unstructured highly charged regions on the stability and specificity of dimerization of two-stranded alpha-helical coiled-coils:neck region of kinesin-like motor protein Kif3A [C] . Mundeep S.Chana, Brian P.Tripet, Robert S.Hodges the International Peptide Symposium . 2001

机译：非结构化高度充电区域对双链α-螺旋卷绕线圈二聚化的稳定性和特异性的作用：Kinesin样电机蛋白kif3a的颈部区域
5. Studies of electrostatic, salt, and metal-binding interactions in the alpha-helical coiled-coil: A model protein system [D] . Kohn, Wayne David 1998

机译：α-螺旋卷曲螺旋中静电，盐和金属结合相互作用的研究：一种模型蛋白质系统
6. Presence of two distinct regions in the coiled-coil structure of the streptococcal Pep M5 protein: relationship to mammalian coiled-coil proteins and implications to its biological properties. [O] . B N Manjula, B L Trus, V A Fischetti 1985

机译：链球菌Pep M5蛋白的卷曲螺旋结构中存在两个不同的区域：与哺乳动物卷曲螺旋蛋白的关系及其生物学特性。
7. Streptococcal M protein: alpha-helical coiled-coil structure and arrangement on the cell surface. [O] . Phillips, G N, Flicker, P F, Cohen, C, 1981

机译：链球菌M蛋白：α-螺旋卷曲螺旋结构及其在细胞表面的排列。

Streptococcal M protein: alpha-helical coiled-coil structure and arrangement on the cell surface.

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