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

FEBS Letters
Fernando Martín-GarcíaPaulino Gómez-Puertas

Abstract

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.

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Citations

Mar 22, 2014·Soft Matter·Pablo González de Prado SalasPedro Tarazona
Jul 11, 2013·Langmuir : the ACS Journal of Surfaces and Colloids·Mario EncinarMarisela Vélez
Sep 4, 2015·The Journal of Biological Chemistry·Estefanía SalvarelliAna Isabel Rico
May 14, 2016·Physical Review. E·Pablo González de Prado Salas, Pedro Tarazona

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