3.6.5.3: protein-synthesizing GTPase
This is an abbreviated version!
For detailed information about protein-synthesizing GTPase, go to the full flat file.
Word Map on EC 3.6.5.3
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3.6.5.3
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gtpases
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eif4e
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spacer
-
ras
-
actin
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rapamycin
-
1-alpha
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gdp
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aminoacyl-trnas
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mtor
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rrna
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perk
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clade
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fusarium
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potato
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conidia
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chop
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reticulocyte
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dextrose
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polysomes
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rna-dependent
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gtp-binding
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aminoacylated
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cap-dependent
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adp-ribosylation
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pausing
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monophyletic
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oxysporum
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wilt
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cdc42
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beta-tubulin
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stall
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autophosphorylation
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normfinder
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atf6
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rinsed
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gdp-bound
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reisolated
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neurofibromatosis
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sh2
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preinitiation
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discolor
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interferon-induced
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anticodons
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p21ras
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genorm
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diphtheria
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rnapii
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hyaline
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caspase-12
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medicine
- 3.6.5.3
- gtpases
- eif4e
-
spacer
- ras
- actin
- rapamycin
-
1-alpha
- gdp
- aminoacyl-trnas
- mtor
- rrna
-
perk
- clade
- fusarium
- potato
- conidia
-
chop
- reticulocyte
- dextrose
- polysomes
-
rna-dependent
-
gtp-binding
-
aminoacylated
-
cap-dependent
-
adp-ribosylation
-
pausing
-
monophyletic
- oxysporum
-
wilt
- cdc42
- beta-tubulin
-
stall
- autophosphorylation
-
normfinder
- atf6
-
rinsed
-
gdp-bound
-
reisolated
- neurofibromatosis
- sh2
-
preinitiation
-
discolor
-
interferon-induced
-
anticodons
-
p21ras
-
genorm
- diphtheria
- rnapii
-
hyaline
- caspase-12
- medicine
Reaction
Synonyms
50S ribosomal subunit assembly factor, aEF-1alpha, aIF2, aIF2 GTPase, aIF2-gamma, aIF2B, aIF2gamma, aIF5B, archaeal initiation factor 2, archaeal initiation factor 2C, archaeal translation initiation factor 2, BipA, BPI-inducible protein A, Bst-IF2, chloroplast elongation factor G, EC 3.6.1.48, Ec-L10, Ec-L11, Ec-L12, Eco-IF2, eEF1A, eEF2, EF 1 alpha, EF-1alpha, EF-1beta, EF-2, EF-4, EF-G, EF-G GTPase, EF-G1, EF-G1mt, EF-like GTPase, EF-Tu, EF-Tumt, EF4, EFL, Efl1, Efl1 GTPase, eIEF2, eIF 2, eIF2, eIF2A, eIF2alpha, eIF2B, eIF5, eIF5B, elongation factor, elongation factor (EF), elongation factor 1 alpha, elongation factor 1alpha, elongation factor 2, elongation factor 4, elongation factor G, elongation factor thermo unstable, elongation factor Tu, elongation factor-1alpha, elongation factor-1beta, elongation factor-2, elongation factor-like 1, elongation factor-like 1 GTPase, eukaryotic elongation factor 2, eukaryotic elongation factor one alpha, eukaryotic initiation factor 2, eukaryotic initiation factor 2A, eukaryotic initiation factor 5B, eukaryotic translation initiation factor 2, eukaryotic translation initiation factor 5B, fusA, GTP phosphohydrolase, GTPase, GTPase aIF5B, GTPase HflX, GTPase-activating protein, guanine triphosphatase, guanine-nucleotide-exchange factor of eIF2, guanosine 5'-triphosphatase, guanosine triphosphatase, HflX, HflX GTPase, IF-2, IF1, IF2, IF2 GTPase, IF2alpha, IF3, IF5B, infB, initiation factor (IF), initiation factor 2, initiation factor 3, initiation factor 5B, initiation factor aIF5B, initiation factor-2, L10, L11, L12, LepA, mitochondrial elongation factor G, mitochondrial initiation factor 2, peptide-release or termination factor, protein-synthesizing GTPase, protein-sythesizing GTPase, RF3, ribosomal GTPase, ribosome-bound initiation factor 2, ribosome-dependent GTPase, SelB, selenocysteine tRNA-specific elongation factor, signal recognition particle GTPase Ffh, SRP GTPase Ffh, Ss-aIF2, SsEF-1alpha, SsEF-2, SsGBP, SSO0269, SSO0412, SSO1050, SSO2381, SsoHflX, translation elongation factor 2, translation factor aIF2/5B, translation initiation factor, translation initiation factor 2, translation initiation factor 2 gamma, translation initiation factor 5B, translation initiation factor eIF5, translation initiation factor IF1, translation initiation factor IF2, translation termination factor eRF3, translational GTPase, translational guanosine triphosphatase, translational initiation factor 2, trGTPase, Tt-L11, ymIF2
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3.6.5.3 protein-synthesizing GTPaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.6.5.3 - protein-synthesizing GTPase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2',3'-O-N'-methylanthranilate-GTP + H2O
2',3'-O-N'-methylanthranilate-GDP + phosphate
-
2',3'-O-N'-methylanthranilate, i.e. mant, is attached to GTP. EF-G binds and efficiently hydrolyzes mant-GTP in a ribosome-dependent manner
-
-
?
GTP gamma-(p-azido)anilide + H2O
GDP + phosphoric acid p-azidoanilin
-
-
-
?
GTP + H2O
?
-
70S ribosome, ribosome recycling factor, EF-G, GTP, 30°C, 15 min
-
-
r
GTP + H2O
?
-
70S ribosome, ribosome recycling factor, EF-G, GTP, 30°C, 15 min
-
-
r
GTP + H2O
GDP + phosphate
-
-
-
-
?
GTP + H2O
GDP + phosphate
-
IF2 in complex with GTP, but not GDP promotes fast association of ribosomal subunits during initiation. IF2 promotes fast formation of the first peptide bond in the presence of GTP, but not GDP. GTP form of IF2 accelerates formation of the 70S ribosome from subunits and GTP hydrolysis accelerates release of IF2 from the 70S ribosome
-
-
?
GTP + H2O
GDP + phosphate
-
importance of GTP hydrolysis in translation initiation for optimal cell growth
-
-
?
GTP + H2O
GDP + phosphate
-
release of peptide promoted by the GGQ motif of class 1 release factors regulates the GTPase activity of RF3. Binding of GTP to RF3 and GTP hydrolysis requires peptide chain release
-
-
?
GTP + H2O
GDP + phosphate
-
the catalytic role of His84 in elongation factor Tu is to stabilize the transition state of GTP hydrolysis by hydrogen bonding to the attacking water molecule or, possibly, the gamma-phosphate group of GTP
-
-
?
GTP + H2O
GDP + phosphate
-
the integrity of the path between the peptidyltransferase center and both GTPase-associated center and sarcin-ricin loop is important for EF-G binding
-
-
?
GTP + H2O
GDP + phosphate
-
reaction using Escherichia coli 70S ribosomes, determination of binding of GTPases to 70S ribosomes in the GTP state, formation of 70S ribosome-tRNAPhe -GTPase-GDPNP complexes, multiple-turnover GTP hydrolysis
-
-
?
GTP + H2O
GDP + phosphate
after GTP hydrolysis and phosphate release, the loss of interactions between the nucleotide and the switch 1 loop of EF-Tu allows domain D1 of EF-Tu to rotate relative to domains D2 and D3 and leads to an increased flexibility of the switch 1 loop. This rotation induces a closing of the D1-D3 interface and an opening of the D1-D2 interface. The opening of the D1-D2 interface, which binds the CCA tail of the tRNA, weakens the crucial EF-Tu-tRNA interactions, which lowers tRNA binding affinity, representing the first step of tRNA release
-
-
?
GTP + H2O
GDP + phosphate
-
reaction using Escherichia coli 70S ribosomes, determination of binding of GTPases to 70S ribosomes in the GTP state, formation of 70S ribosome-tRNAPhe -GTPase-GDPNP complexes, multiple-turnover GTP hydrolysis
-
-
?
GTP + H2O
GDP + phosphate
-
extodomain 2+3 stimulate the GTPase activity of ectodomain 1
-
-
?
GTP + H2O
GDP + phosphate
-
extodomain 2+3 suppress the GTPase activity of ectodomain 1
-
-
?
GTP + H2O
GDP + phosphate
-
GTPase activation due to C domain of the translation termination factor eRF1, which is bound with translation termination factor eRF3. As for the M and N domains, stimulation of eRF3 GTPase activity is more likely associated with the former, which is located in the large subunit along with the GTPase center of the ribosome, than with the latter, which is oriented towards the decoding center located in the small ribosomal subunit
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-
?
GTP + H2O
GDP + phosphate
-
the selenocysteine tRNA-specific elongation factor is responsible for the cotranslational incorporation of selenocysteine into proteins by recoding of a UGA step codon in the presence of a downstream mRNA hairpin loop
-
-
?
GTP + H2O
GDP + phosphate
-
two models of the reaction mechanism using the crystal structure: I. Glu81 becomes protonated upon GTP binding, with preference to bind GDP apparently contradicting its assignment as ON, or II. Glu81 protonation/deprotonation defines the ON/OFF states. Protonated Glu81, is ON, whereas X-ray(GTP):GDP is OFF. The model postulates that distant conformational changes such as domain IV rotation are uncoupled from GTP/GDP exchange and do not affect the relative GTP/GDP binding affinities. Glu81-GTP interaction helps to hold switch 2 in place, if Glu81 is deprotonated, it and nearby residues move away from their crystal positions
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
?
GTP + H2O
GDP + phosphate
-
ribosome-dependent GTPase strongly stimulates the binding of initiator tRNA to the ribosomes even in the absence of other factors
-
-
?
GTP + H2O
GDP + phosphate
-
aIF2/5B enhances the translation of both leadered and leaderless mRNAs when expressed in a cell-free protein-synthesizing system
-
-
?
GTP + H2O
GDP + phosphate
ATP hydrolysis is insignificant compared to the levels of GTP hydrolysis
-
-
?
GTP + H2O
GDP + phosphate
-
displays either the intrinsic or the ribosome-dependent GTPase activity
-
-
?
GTP + H2O
GDP + phosphate
slow GTPase with relatively low affinity for GTP
-
-
?
GTP + H2O
GDP + phosphate
GTP hydrolysis by subunit aIF2gamma
-
-
?
GTP + H2O
GDP + phosphate
aIF2 significantly hydrolyses GTP in vitro, GTP hydrolysis by aIF2 or by its isolated gamma subunit. Assay with aIF2-Met-tRNAfMet enzyme complex and GTP
-
-
?
GTP + H2O
GDP + phosphate
GTP hydrolysis by subunit aIF2gamma
-
-
?
GTP + H2O
GDP + phosphate
aIF2 significantly hydrolyses GTP in vitro, GTP hydrolysis by aIF2 or by its isolated gamma subunit. Assay with aIF2-Met-tRNAfMet enzyme complex and GTP
-
-
?
GTP + H2O
GDP + phosphate
GTP hydrolysis by subunit aIF2gamma
-
-
?
GTP + H2O
GDP + phosphate
aIF2 significantly hydrolyses GTP in vitro, GTP hydrolysis by aIF2 or by its isolated gamma subunit. Assay with aIF2-Met-tRNAfMet enzyme complex and GTP
-
-
?
GTP + H2O
GDP + phosphate
GTP hydrolysis by subunit aIF2gamma
-
-
?
GTP + H2O
GDP + phosphate
aIF2 significantly hydrolyses GTP in vitro, GTP hydrolysis by aIF2 or by its isolated gamma subunit. Assay with aIF2-Met-tRNAfMet enzyme complex and GTP
-
-
?
GTP + H2O
GDP + phosphate
GTP hydrolysis by subunit aIF2gamma
-
-
?
GTP + H2O
GDP + phosphate
aIF2 significantly hydrolyses GTP in vitro, GTP hydrolysis by aIF2 or by its isolated gamma subunit. Assay with aIF2-Met-tRNAfMet enzyme complex and GTP
-
-
?
GTP + H2O
GDP + phosphate
ATP hydrolysis is insignificant compared to the levels of GTP hydrolysis
-
-
?
GTP + H2O
GDP + phosphate
slow GTPase with relatively low affinity for GTP
-
-
?
GTP + H2O
GDP + phosphate
-
the enzyme has the same domain structure and biochemical properties of a typical IF2 species as found in bacteria or mammalian mitochondria, but with enhanced ability to bind unformylated initiator met-tRNA
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
mutant of elongation factor G containing the effector loop from Thermus aquaticus EF-Tu has markedly decreased GTPase activity and does not catalyze translocation. The loops are not functionally interchangeable since the factors interact with different states of the ribosome
-
-
?
GTP + H2O
GDP + phosphate
-
Base A 2660 is crucial for GTPase activity of EF-G. Reaction rates using reconstituted ribosomes, single turnover measurement, overview
-
-
?
GTP + H2O
GDP + phosphate
after GTP hydrolysis and phosphate release, the loss of interactions between the nucleotide and the switch 1 loop of EF-Tu allows domain D1 of EF-Tu to rotate relative to domains D2 and D3 and leads to an increased flexibility of the switch 1 loop. This rotation induces a closing of the D1-D3 interface and an opening of the D1-D2 interface. The opening of the D1-D2 interface, which binds the CCA tail of the tRNA, weakens the crucial EF-Tu-tRNA interactions, which lowers tRNA binding affinity, representing the first step of tRNA release
-
-
?
GTP + H2O
GDP + phosphate
-
mutant of elongation factor G containing the effector loop from Thermus aquaticus EF-Tu has markedly decreased GTPase activity and does not catalyze translocation. The loops are not functionally interchangeable since the factors interact with different states of the ribosome
-
-
?
GTP + H2O
GDP + phosphate
-
elongation factor G catalyzes the translocation step in protein synthesis on the ribosome
-
-
?
GTP + H2O
GDP + phosphate
-
enzyme-GTP and enzyme-GDP conformations in solution are very similar. The major contribution to the active GTPase conformation, which is quite different, therefore comes from its interaction with the ribosome
-
-
?
GTP + H2O
GDP + phosphate
-
EF-Tu is in its active conformation, when the switch I loop is ordered, and the catalytic histidine is coordinating the nucleophilic water in position for inline attack on the gamma-phosphate of GTP. The activated conformation is achieved due to a critical and conserved interaction of the histidine with A2662 of the sarcin-ricin loop of the 23S ribosomal RNA. Universal mechanism for GTPase activation and hydrolysis in translational GTPases on the ribosome. Premature GTP hydrolysis in EF-Tu is prevented by a hydrophobic gate consisting of residues Val20 of the P loop and Ile60 of switch I, which restricts access of His84 to the catalytic water
-
-
?
GTP + H2O
GDP + phosphate
molecular recognition in the GTP-binding site, overview
-
-
?
GTP + H2O
GDP + phosphate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
EF-Tu is in its active conformation, when the switch I loop is ordered, and the catalytic histidine is coordinating the nucleophilic water in position for inline attack on the gamma-phosphate of GTP. The activated conformation is achieved due to a critical and conserved interaction of the histidine with A2662 of the sarcin-ricin loop of the 23S ribosomal RNA. Universal mechanism for GTPase activation and hydrolysis in translational GTPases on the ribosome. Premature GTP hydrolysis in EF-Tu is prevented by a hydrophobic gate consisting of residues Val20 of the P loop and Ile60 of switch I, which restricts access of His84 to the catalytic water
-
-
?
GTP + H2O
GDP + phosphate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
molecular recognition in the GTP-binding site, overview
-
-
?
GTP + H2O
GDP + phosphate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
GDP binding structure analysis
-
?
guanosine 5'-(thio)triphosphate + H2O
GDP + thiophosphate + 3 H+
-
-
-
?
guanosine 5'-(thio)triphosphate + H2O
GDP + thiophosphate + 3 H+
-
-
-
?
additional information
?
-
-
EF4-ribosome interactions during reverse translocation, overview
-
-
?
additional information
?
-
-
residue 196 is located in a solvent-exposed location of the G' subdomain, while its neighboring helices AG' and BG' make contacts with protein L7/L12 of the ribosome. The latter contacts involve conserved electrostatically interacting residues that allosterically activate GTP hydrolysis in the G domain of EF-G. Residue 58 moves substantially from its initial ordered position adjacent to helix BIII
-
-
?
additional information
?
-
-
EF-G binding, without GTP hydrolysis, promotes slow and possibly incomplete translocation
-
-
?
additional information
?
-
enzyme-ribosome binding analysis, overview. Binding of wild-type EF4 and mutant variants to the ribosome in the presence of guanine nucleotides, kinetics and affinities
-
-
?
additional information
?
-
apo-form, and GDP- and nonhydrolysable GTP analogue guanosine-3',5'-bisdiphosphate (ppGpp)-bound BipA, structure analysis, overview
-
-
-
additional information
?
-
contacts between EF-G, protein S12, and helices 43 and 44 of 23S ribosomal RNA. Escherichia coli strain MRE600 70S ribosomes are used as substrates
-
-
-
additional information
?
-
formation of the 70S-fMet-tRNAi Met-IF2-GDPNP complex. 70S ribosomes are isolated from Escherichia coli strain CAN20, recombinant His-tagged IF2 enzyme, non-hydrolyzable GTP analogue GDPNP
-
-
-
additional information
?
-
-
formation of the 70S-fMet-tRNAi Met-IF2-GDPNP complex. 70S ribosomes are isolated from Escherichia coli strain CAN20, recombinant His-tagged IF2 enzyme, non-hydrolyzable GTP analogue GDPNP
-
-
-
additional information
?
-
IF2 has protein chaperone activity. It catalyzes the refolding of heat-denatured GFP upon incubation for 8 min at 25°C at chaperone/GFP stoichiometric ratios of 1:1 carried out in buffer containing 1 mM GTP and 1 mM ATP. IF2alpha displays the highest chaperone activity in the presence of GTP, and its activity is substantially reduced, albeit not completely abolished, in the presence of GDP, or of the non-hydrolysable analogue GDPCP or in the absence of guanine nucleotides
-
-
-
additional information
?
-
-
IF2 has protein chaperone activity. It catalyzes the refolding of heat-denatured GFP upon incubation for 8 min at 25°C at chaperone/GFP stoichiometric ratios of 1:1 carried out in buffer containing 1 mM GTP and 1 mM ATP. IF2alpha displays the highest chaperone activity in the presence of GTP, and its activity is substantially reduced, albeit not completely abolished, in the presence of GDP, or of the non-hydrolysable analogue GDPCP or in the absence of guanine nucleotides
-
-
-
additional information
?
-
upon GTP hydrolysis, phosphate release results in a loss of the switch 1 loop anchoring to the rest of D1, which frees D1 to rotate around the switch 2 helix. This rotation closes the D1-D3 interface and opens the D2-D3 interface, possibly decreasing the interaction of EF-Tu with the amino acid and the CCA tail of the tRNA and, therefore, the affinity of the tRNA to EF-Tu
-
-
-
additional information
?
-
-
EF4-ribosome interactions during reverse translocation, overview
-
-
?
additional information
?
-
elongation factor eEF2 catalyzes ribosomal reverse translocation at one mRNA triplet. This process requires a cognate tRNA in the ribosomal E-site and cannot occur spontaneously without eEF2. The efficiency of this reaction depends on the concentrations of eEF2 and cognate tRNAs and increases in the presence of nonhydrolyzable GTP analogues. Deacylated tRNAHis, cognate to the E-site codon, to the POST ribosomal complexes along with eEF2-GTP, causes a shift of the main toeprint peak by 3 nt toward the 5' end of the mRNA. POST ribosomes relocate backwards by three nucleotides in the presence of cognate deacylated tRNA and eEF2. Reverse translocation required up to a 20fold excess of eEF2 over the ribosomal complexes, whereas direct translocation is effective at a 2:1 ratio. Model of eEF2-catalyzed reverse translocation, overview
-
-
-
additional information
?
-
P05198; P20042; P41091
substrate eIF2, phosphorylation of the eIF2alpha subunit in response to various cellular stresses converts substrate eIF2 into a competitive inhibitor of eIF2B, which triggers the integrated stress response (ISR)
-
-
-
additional information
?
-
-
GTP/GDP binding analysis using molecular dynamics and a continuum electrostatic free energy method
-
-
?
additional information
?
-
aIF2 shows very high conformational flexibility in the alpha- and beta-subunits probably required for interaction of aIF2 with the small ribosomal subunit, overview
-
-
?
additional information
?
-
-
aIF2 shows very high conformational flexibility in the alpha- and beta-subunits probably required for interaction of aIF2 with the small ribosomal subunit, overview
-
-
?
additional information
?
-
-
EF-1alpha shows GTPase activity and GDP-binding ability
-
-
?
additional information
?
-
-
HflX interacts with 50S and 70S particles, and also with the 30S subunit, independent of the nucleotide-bound state and in tight binding, minimal model for the functional cycle of HflX, interaction with the 70S ribosome and functional mechanism of HflX, overview
-
-
?
additional information
?
-
-
structure-activity relationship, molecular dynamics simulations, overview
-
-
?
additional information
?
-
-
the enzyme exhibits significant binding activity with the nonformylated Met-tRNAf(Met)
-
-
?
additional information
?
-
-
eIF2A functions as a suppressor of Ure2p internal ribosome entry site-mediated translation in yeast cells
-
-
?
additional information
?
-
-
Met-tRNA + 40S ribosomal subunit {?}
-
-
?
additional information
?
-
-
Met-tRNA + 40S ribosomal subunit {?}
-
-
?
additional information
?
-
-
feeding artificial milk diets stimulate protein synthesis in skeletal muscle and liver of neonatal pigs by modulating the translation initiation factors that regulate mRNA binding to the ribosomal complex. However, provision of a high-protein diet that exceeds the protein requirement does not further enhance protein synthesis or translation initiator factor activation
-
-
?
additional information
?
-
upon GTP hydrolysis, phosphate release results in a loss of the switch 1 loop anchoring to the rest of D1, which frees D1 to rotate around the switch 2 helix. This rotation closes the D1-D3 interface and opens the D2-D3 interface, possibly decreasing the interaction of EF-Tu with the amino acid and the CCA tail of the tRNA and, therefore, the affinity of the tRNA to EF-Tu
-
-
-
additional information
?
-
the G-nucleotide binding pocket includes five G motifs (G1-G5) that are conserved in trGTPase factors. In the ribosome-bound EF4, the G1 motif (residues 18-24) establishes extensive contacts with the triphosphate moiety and ribose sugar of GDPCP. EF4 GTPase activation upon ribosome binding
-
-
-
