Activation of cell division protein FtsZ. Control of switch loop T3 conformation by the nucleotide gamma-phosphate

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 gamma-phosphate of GTP induces a conformational perturbation in loop T...

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Bibliographic Details
Published in:The Journal of biological chemistry 2001-05, Vol.276 (20), p.17307
Main Authors: Díaz, J F, Kralicek, A, Mingorance, J, Palacios, J M, Vicente, M, Andreu, J M
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Archaeal Proteins - chemistry
Archaeal Proteins - genetics
Archaeal Proteins - metabolism
Binding Sites
Cell Division
Glycine
Guanosine Diphosphate - metabolism
Guanosine Triphosphate - metabolism
Methanococcus - cytology
Methanococcus - genetics
Methanococcus - physiology
Models, Molecular
Mutagenesis, Site-Directed
Protein Conformation
Protein Structure, Secondary
Recombinant Proteins - chemistry
Recombinant Proteins - metabolism
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Tubulin - chemistry
Tubulin - metabolism
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Summary: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 gamma-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 gamma-phosphate into a more compact conformation than with GDP, related to that observed in the homologous proteins alpha- and beta-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 A away from gamma-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.
ISSN:0021-9258
DOI:10.1074/jbc.M010920200