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J. Biol. Chem., Vol. 276, Issue 20, 17307-17315, May 18, 2001
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From the 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
Activation of Cell Division Protein FtsZ
CONTROL OF SWITCH LOOP T3 CONFORMATION BY THE NUCLEOTIDE
-PHOSPHATE*
§,,,
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
-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.
*
This work was supported in part by Comisión
Interministerial de Ciencia y Tecnología (Spain) Grants
BIO99-0859-C03-02-03 and BIO97-1246 and by Programa de Grupos
Estratégicos de la Comunidad Autónoma de Madrid.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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