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首页> 外文期刊>Journal of Molecular Biology >Diversity of structural behavior in vertebrate conventional myosins complexed with actin.
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Diversity of structural behavior in vertebrate conventional myosins complexed with actin.

机译：脊椎动物常规肌球蛋白与肌动蛋白复合的结构行为的多样性。

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摘要

Low-resolution three-dimensional structures of acto-myosin subfragment-1 (S1) complexes were retrieved from X-ray fiber diffraction patterns, recorded either in the presence or absence of ADP. The S1 was obtained from various myosin-II isoforms from vertebrates, including rabbit fast-skeletal and cardiac, chicken smooth and human non-muscle IIA and IIB species, and was diffused into an array of overstretched, skinned skeletal muscle fibers. The S1 attached to the exposed actin filaments according to their helical symmetry. Upon addition of ADP, the diffraction patterns from acto-S1 showed an increasing magnitude of response in the order as listed above, with features of a lateral compression of the whole diffraction pattern (indicative of increased radius of the acto-S1 complex) and an enhancement of the fifth layer-line reflection. The structure retrieval indicates that these changes are mainly due to the swing of the light chain (LC) domain in the direction consistent with the cryo-electron microscopic results. In the non-muscle isoforms, the swing is large enough to affect the manner of quasi-crystal packing of the S1-decorated actin filaments and their lattice dimension, with a small change in the twist of actin filaments. Variations also exist in the behavior of the 50K-cleft, which apparently opens upon addition of ADP to the non-muscle isoforms but not to other isoforms. The fast-skeletal S1 remains as the only isoform that does not clearly exhibit either of the structural changes. The results indicate that the "conventional" myosin-II isoforms exhibit a wide variety of structural behavior, possibly depending on their functions and/or the history of molecular evolution.
机译：从X射线纤维衍射图谱中检索到肌动球蛋白亚片段1（S1）复合物的低分辨率三维结构，并记录是否存在ADP。 S1获自脊椎动物的各种肌球蛋白-II同工型，包括兔快速骨骼和心脏，鸡平滑肌和人非肌肉IIA和IIB物种，并扩散到一系列过度拉伸的皮肤骨骼肌纤维中。 S1根据其螺旋对称性附着在暴露的肌动蛋白丝上。添加ADP后，来自acto-S1的衍射图谱按上述顺序显示出响应幅度的增加，具有整个衍射图谱的侧向压缩（表明acto-S1络合物半径增大）和增强第五层线反射。结构检索表明，这些变化主要归因于轻链（LC）域在与低温电子显微镜结果一致的方向上的摆动。在非肌肉同工型中，摆动大到足以影响S1装饰的肌动蛋白丝的准晶体堆积方式及其晶格尺寸，而肌动蛋白丝的捻度变化很小。 50K裂口的行为也存在变化，显然是在将ADP添加到非肌肉同工型而不是其他同工型时打开的。快速骨骼肌S1保留为唯一没有清楚显示任何结构变化的同工型。结果表明“常规的”肌球蛋白-II同工型表现出各种各样的结构行为，这可能取决于它们的功能和/或分子进化的历史。

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