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首页> 外文期刊>Journal of Molecular Biology >Structural Change in the Dynein Stalk Region Associated with Two Different Affinities for the Microtubule
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Structural Change in the Dynein Stalk Region Associated with Two Different Affinities for the Microtubule

机译：与微管两种不同亲和力相关的Dynein茎区域的结构变化

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Dynein is a large microtubule-based motor complex that requires tight coupling of intra-molecular ATP hydrolysis with the generation of mechanical force and track-binding activity. However, the microtubule-binding domain is structurally separated by about 15 nm from the nucleotide-binding sites by a coiled-coil stalk. Thus, long-range two-way communication is necessary for coordination between the catalytic cycle of ATP hydrolysis and dynein's track-binding affinities. To investigate the structural changes that occur in the dynein stalk region to produce two different microtubule affinities, here we improve the resolution limit of the previously reported structure of the entire stalk region and we investigate structural changes in the dynein stalk and strut/buttress regions by comparing currently available X-ray structures. In the light of recent crystal structures, the basis of the transition from the low-affinity to the high-affinity coiled-coil registry is discussed. A concerted movement model previously reported by Carter and Vale is modified more specifically, and we proposed it as the open zipper model. (C) 2015 Elsevier Ltd. All rights reserved.
机译：Dynein是一种基于大的基于微管的电动机综合体，需要通过产生机械力和轨道结合活性的分子内ATP水解的紧密耦合。然而，通过卷绕线圈茎茎从核苷酸结合位点通过约15nm结构，微管结合结构域在结构上分离。因此，远程双向通信对于ATP水解和Dynein结合亲和力的催化循环之间的配位是必要的。为了探讨在Dynein茎区产生两种不同的微管亲和力的结构变化，这里我们改善了先前报道的整个茎区结构的分辨率限制，并研究了Dynein茎秆和支柱/支撑区域的结构变化比较目前可用的X射线结构。鉴于最近的晶体结构，讨论了从低亲和力与高亲和力盘管注册表的过渡的基础。由Carter和Vale报告的一级运动模型更具体地修改，我们提出了它作为开放拉链模型。 （c）2015 Elsevier Ltd.保留所有权利。

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