Identification of the key interactions in structural transition pathway of FtsZ from Staphylococcus aureus
Identification of the key interactions in structural transition pathway of FtsZ from Staphylococcus aureus
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DOI：
10.1016/j.jsb.2017.04.008
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发表时间：
2017-05-01
影响因子：
3
通讯作者：
Matsumura, Hiroyoshi
中科院分区：
文献类型：
--
作者：
Fujita, Junso;Harada, Ryuhei;Matsumura, Hiroyoshi
微管蛋白同源蛋白FtsZ是细菌细胞分裂所必需的。FtsZ聚合形成原丝，在GTP存在下组装成可收缩的环状结构。最近的研究表明，FtsZ双酶切结合GT3活性驱动细胞壁合成和细菌细胞分裂。FtsZ的组装和分解引起的双磨与单体从紧张（T）到松弛（R）状态的构象变化有关，但关于其机制仍存在相当大的争议。在这项研究中，我们报告的晶体结构的FtsZ从金黄色葡萄球菌对应的T和R状态构象在同一晶体中，表明两个状态的结构平衡。这两个结构确定了一个关键残基Arg29，其重要性也证实了我们的修改后的MD模拟。R29 A突变体的晶体结构显示出T和R状态样构象，与野生型相比，具有轻微但重要的结构变化。总的来说，这些数据为理解分子内相互作用如何与FtsZ的结构转变相关提供了新的见解。(C)2017爱思唯尔公司All rights reserved.
The tubulin-homolog protein FtsZ is essential for bacterial cell division. FtsZ polymerizes to form protofilaments that assemble into a contractile ring-shaped structure in the presence of GTP. Recent studies showed that FtsZ treadmilling coupled with the GTPase activity drives cell wall synthesis and bacterial cell division. The treadmilling caused by assembly and disassembly of FtsZ links to a conformational change of the monomer from a tense (T) to a relaxed (R) state, but considerable controversy still remains concerning the mechanism. In this study, we report crystal structures of FtsZ from Staphylococcus aureus corresponding to the T and R state conformations in the same crystal, indicating the structural equilibrium of the two state. The two structures identified a key residue Arg29, whose importance was also confirmed by our modified MD simulations. Crystal structures of the R29A mutant showed T and R state-like conformations with slight but important structural changes compared to those of wild-type. Collectively, these data provide new insights for understanding how intramolecular interactions are related to the structural transition of FtsZ. (C) 2017 Elsevier Inc. All rights reserved.