Molecular dynamics simulation of GTPase activity in polymers of the cell division protein FtsZ

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• 作者：Fernando Martí ; n-Garcí ; a^a ; ^b ; Estefaní ; a Salvarelli^b ; ^c ; Jes&uacute ; s Ignacio Mendieta-Moreno^a ; ^b ; Miguel Vicente^d ; Jes&uacute ; s Mingorance^c ; ^{jesus.mingorance@idipaz.es} ; Jes&uacute ; s Mendieta^a ; ^b ; ¹ ; Paulino Gó ; mez-Puertas^a ; ¹ ; ^{pagomez@cbm.uam.es}
• 关键词：MD ; molecular dynamics
• 刊名：FEBS Letters
• 出版年：2012
• 期刊代码：70_00145793
• 类别：bio
• 出版时间：24 April, 2012
• 卷：586
• 期：8
• 页码：1236-1239
• 文件大小：1049 K

摘要

FtsZ, the prokaryotic ortholog of tubulin, assembles into polymers in the bacterial division ring. The interfaces between monomers contain a GTP molecule, but the relationship between polymerization and GTPase activity is not unequivocally proven. A set of short FtsZ polymers were modelled and the formation of active GTPase structures was monitored using molecular dynamics. Only the interfaces nearest the polymer ends exhibited an adequate geometry for GTP hydrolysis. Simulated conversion of interfaces from close-to-end to internal position and vice versa resulted in their spontaneous rearrangement between active and inactive conformations. This predicted behavior of FtsZ polymer ends was supported by in vitro experiments.