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3.6.5.6: tubulin GTPase

This is an abbreviated version!
For detailed information about tubulin GTPase, go to the full flat file.

Word Map on EC 3.6.5.6

Reaction

GTP
+
H2O
=
GDP
 +
phosphate

Synonyms

atypical GTPase, BtubB, cell division protein, EC 3.6.1.51, eFtsZ, FtsZ, FtsZ tubulin-like protein, FtsZDr, gamma-tubulin, GTP phosphohydrolase, GTPase, guanine triphosphatase, guanosine 5'-triphosphatase, guanosine triphosphatase, mFtsZ, ORF156, ribosomal GTPase, TUBG1, tubulin, tubulin FtsZ, tubulin GTPase, tubulin homolog FtsZ, tubulin-colchicine GTPase

ECTree

     3 Hydrolases
         3.6 Acting on acid anhydrides
             3.6.5 Acting on GTP to facilitate cellular and subcellular movement
                3.6.5.6 tubulin GTPase

Engineering

Engineering on EC 3.6.5.6 - tubulin GTPase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D158A
site-directed mutagenesis, altered directional movement of FtsI and septal PG composition in FtsZmut cells
D212G
site-directed mutagenesis, altered directional movement of FtsI and septal PG composition in FtsZmut cells
D269A
site-directed mutagenesis
E238A
site-directed mutagenesis
E250A
site-directed mutagenesis, altered directional movement of FtsI and septal PG composition in FtsZmut cells
G105S
site-directed mutagenesis
D158A
-
site-directed mutagenesis, altered directional movement of FtsI and septal PG composition in FtsZmut cells
-
D269A
-
site-directed mutagenesis
-
E238A
-
site-directed mutagenesis
-
E250A
-
site-directed mutagenesis, altered directional movement of FtsI and septal PG composition in FtsZmut cells
-
C13A
site-directed mutagenesis, mutation of Cyst13 to Ala (GFP-A13gamma-tubulinresist) impairs GTP binding to the GTPase domain, stable co-expresses of the mutated recombinant protein in gamma-tubulin sh-U2-OS cells
R399A/K400A/R409A
site-directed mutagenesis
C354A
-
site-directed mutagenesis of beta-tubulin, the mutation dramatically reduces the rate of microtubule shrinking and the frequency of catastrophe
C354S
-
site-directed mutagenesis of beta-tubulin, the mutation dramatically reduces the rate of microtubule shrinking and the frequency of catastrophe
T143G
-
mutation in tubulin signature motif of beta-tubulin, both GTP-binding affinity and microtubule-dependent GTPase activity are reduced at least 15 fold, mutant cells have a delay in mitosis
T238A
-
naturally occuring mutation, the buried mutation T238A in alphabeta-tubulin yields microtubules with dramatically reduced shrinking rate and catastrophe frequency, the mutation uncouples the tubulin conformational and GTPase cycles, revealing allosteric control of microtubule dynamics. The mutation causes these effects by suppressing a conformational change that normally occurs in response to GTP hydrolysis in the lattice, without detectably changing the conformation of unpolymerized alphabetab-tubulin. The mutation predominantly affects post-GTPase conformational and dynamic properties of microtubules. The buried T238A mutation in beta-tubulin hyperstablizes microtubules in vivo and in vitro. Mutant-induced changes in polymerization dynamics do not result from defective GTPase activity. The T238A alphabeta-tubulin undergoes spontaneous nucleation more readily than wild-type, even in the presence of a nonhydrolyzable GTP analog, GTPgammaS, phenotype, overview
additional information