Intrinsic Bending of Microtubule Protofilaments
Intrinsic Bending of Microtubule Protofilaments
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DOI：
10.1016/j.str.2010.12.020
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发表时间：
2011-03-09
期刊：
影响因子：
5.7
通讯作者：
Voth, Gregory A.
中科院分区：
文献类型：
--
作者：
Grafmueller, Andrea;Voth, Gregory A.
微管（MT）正末端的复杂聚合动力学与结合至β-微管蛋白的GTP核苷酸的水解密切相关。不稳定被认为是与微管蛋白二聚体的构象变化，从直的构象在MT晶格弯曲的构象。它仍然在辩论中是否这种转变是直接相关的核苷酸状态，或MT晶格中的纵向或横向接触的后果。在这里，我们提出了大规模的原子模拟短微管蛋白原丝与核苷酸状态，从两个极端的构象。我们的模拟表明，GDP和GP结合的微管蛋白二聚体和溶液中的原丝中的二聚体间和二聚体内接触都发生弯曲。在GTP和GDP结合的微管蛋白或intradime和interdimer界面的接触的介观性质之间没有可观察到的差异。
The complex polymerization dynamics of the microtubule (MT) plus end are closely linked to the hydrolysis of the GTP nucleotide bound to the beta-tubulin. The destabilization is thought to be associated with the conformational change of the tubulin dimers from the straight conformation in the MT lattice to a curved conformation. It remains under debate whether this transformation is directly related to the nucleotide state, or a consequence of the longitudinal or lateral contacts in the MT lattice. Here, we present large-scale atomistic simulations of short tubulin protofilaments with both nucleotide states, starting from both extreme conformations. Our simulations indicate that both interdimer and intradimer contacts in both GDP and GTP-bound tubulin dimers and protofilaments in solution bend. There are no observable differences between the mesoscopic properties of the contacts in GTP and GDP-bound tubulin or the intradime and interdimer interfaces.