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J. Biol. Chem., Vol. 276, Issue 20, 17307-17315, May 18, 2001

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Activation of Cell Division Protein FtsZ
CONTROL OF SWITCH LOOP T3 CONFORMATION BY THE NUCLEOTIDE -PHOSPHATE^*

José Fernando Díaz^§, Andrew Kralicek, Jesús Mingorance^¶, Juan Manuel Palacios, Miguel Vicente^¶, and José Manuel Andreu

From the  Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas, C/Velázquez, 144, 28006 Madrid and the ^¶ Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas-Campus de Cantoblanco, 28049 Madrid, Spain

The effect of bound nucleotide on the conformation of cell division protein FtsZ from Methanococcus jannaschii has been investigated using molecular dynamics and site-directed mutagenesis. The molecular dynamics indicate that the -phosphate of GTP induces a conformational perturbation in loop T3 (Gly⁸⁸-Gly⁹⁹ segment), in a position structurally equivalent to switch II of Ha-ras-p21. In the simulated GTP-bound state, loop T3 is pulled by the -phosphate into a more compact conformation than with GDP, related to that observed in the homologous proteins - and -tubulin. The existence of a nucleotide-induced structural change in loop T3 has been confirmed by mutating Thr⁹² into Trp (T92W-W319Y FtsZ). This tryptophan (12 Å away from -phosphate) shows large differences in fluorescence emission, depending on which nucleotide is bound to FtsZ monomers. Loop T3 is located at a side of the contact interface between two FtsZ monomers in the current model of FtsZ filament. Such a structural change may bend the GDP filament upon hydrolysis by pushing against helix H8 of next monomer, thus, generating force on the membrane during cell division. A related curvature mechanism may operate in tubulin activation.

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