The Determinants That Govern Microtubule Assembly from the Atomic Structure of GTP-Tubulin
The Determinants That Govern Microtubule Assembly from the Atomic Structure of GTP-Tubulin
复制标题
DOI：
10.1016/j.jmb.2011.07.029
复制
发表时间：
2011-09-09
影响因子：
5.6
通讯作者：
Gigant, Benoit
中科院分区：
文献类型：
--
作者：
Nawrotek, Agata;Knossow, Marcel;Gigant, Benoit
微管蛋白在可溶性弯曲结构和微管直构象之间交替。GTP与α - β -微管蛋白结合是微管组装所必需的，但这是否会引发转化为更直的结构仍存在争议。这至少部分是由于在组装前缺乏gtp -微管蛋白的结构数据。在这里，我们报道了可溶性微管蛋白在GDP和GTP核苷酸状态下的原子分辨率晶体结构。这些结构在核苷酸附近有局部差异。gtp结合的微管蛋白中的环运动有利于其招募到生长的微管的末端，并促进其弯曲到直的转变，但这种转换尚未进行。因此，这些数据表明，构象的变化趋向于直线。结构发生的微管特定的接触建立。他们还提出了微管结构与微管组装相关的修改方式的模型。(C) 2011 Elsevier Ltd.版权所有。
Tubulin alternates between a soluble curved structure and a microtubule straight conformation. GTP binding to alpha beta-tubulin is required for microtubule assembly, but whether this triggers conversion into a straighter structure is still debated. This is due, at least in part, to the lack of structural data for GTP-tubulin before assembly. Here, we report atomic-resolution crystal structures of soluble tubulin in the GDP and GTP nucleotide states in a complex with a stathmin-like domain. The structures differ locally in the neighborhood of the nucleotide. A loop movement in GTP-bound tubulin favors its recruitment to the ends of growing microtubules and facilitates its curved-to-straight transition, but this conversion has not proceeded yet. The data therefore argue for the conformational change toward the straight. structure occurring as microtubule-specific contacts are established. They also suggest a model for the way the tubulin structure is modified in relation to microtubule assembly. (C) 2011 Elsevier Ltd. All rights reserved.