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浙江大学最新Science文章
【字体: 大 中 小 】 时间:2013年07月26日 来源:浙江大学
编辑推荐:
浙江大学生命科学研究院叶升课题组发表了题为“FtsZ protofilaments use a hinge-opening mechanism for constrictive force generation”的文章,第一次解析了细胞分裂蛋白FtsZ所形成的原丝纤维的三维结构,这将为广谱抗生素的研发提供依据。
原文摘要:
FtsZ Protofilaments Use a Hinge-Opening Mechanism for Constrictive Force Generation
The essential bacterial protein FtsZ is a guanosine triphosphatase that self-assembles into a structure at the division site termed the “Z ring”. During cytokinesis, the Z ring exerts a constrictive force on the membrane by using the chemical energy of guanosine triphosphate hydrolysis. However, the structural basis of this constriction remains unresolved. Here, we present the crystal structure of a guanosine diphosphate–bound Mycobacterium tuberculosis FtsZ protofilament, which exhibits a curved conformational state. The structure reveals a longitudinal interface that is important for function. The protofilament curvature highlights a hydrolysis-dependent conformational switch at the T3 loop that leads to longitudinal bending between subunits, which could generate sufficient force to drive cytokinesis.
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