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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

Reaction

GTP
+
H2O
=
GDP
 +
phosphate

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

ECTree

     3 Hydrolases
         3.6 Acting on acid anhydrides
             3.6.5 Acting on GTP to facilitate cellular and subcellular movement
                3.6.5.3 protein-synthesizing GTPase

Crystallization

Crystallization on EC 3.6.5.3 - protein-synthesizing GTPase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant C-terminally His6-tagged enzyme bound to GDP, 10 mg/ml protein and 1.42 mM GDP in buffer C are heated at 70°C for 10 min prior crystallization, sitting drop vapor diffusion method, mixing of 10 mg/ml protein in 10 mM HEPES-KOH, pH 7.6, 100 mM KCl, 10 mM MgCl2, 1.42 GDP, and 7 mM 2-mercaptoethanol with reservoir solution containing 0.1 M Tris-HCl, pH 7.5, 20% w/v PEG 3000, and 0.2 M calcium acetate, at 20°C, 1 week, X-ray diffraction structure determination and analysis at 1.90 A resolution, molecular replacement using the structure of Methanothermobacter thermautotrophicus aIF5B complexed with GDP (PDB ID 1G7S) as the search model
-
sitting drop vapor diffusion method, crystal structure of elongation factor Tu*Ts complex at 2.2 A resolution
-
apo-form, and GDP- and guanosine-3',5'-bisdiphosphate (ppGpp)-bound BipA, X-ray diffraction structure determination and analysis
two crystal forms of a complex between trypsin-modified elongation factor Tu-MgGDP and the antibiotic tetracycline solved by X-ray diffraction analysis to resolution of 2.8 and 2.1 A, respectively
-
hanging-drop vapour-diffusion method
-
vapour-diffusion method from ammonium sulfate either in the presence of GDP, GppHNp or without nucleotide, yielding isomorphous crystals for all three forms
-
crystal structure analysis of enzyme complexed with the GTP analogue GDPNP and with GDP at 2.0 A resolution , PDB IDs 1G7T and 1G7S, enzyme in complex with GTP/Mg2+, modeling and molecular dynamics simulations
-
crystal structure of the regulatory subunit aIF2Balpha, hanging-drop vapour diffusion method at 20°C, three-dimensional structure is determined by X-ray crystallography at 2.2 A resolution
-
5 A resolution crystal structure of the ternary complex formed by archaeal aIF2 from Sulfolobus solfataricus, the GTP analog GDPNP and methionylated initiator tRNA
Q97W59; Q980A5; Q97Z79
analysis of crystal structures of ON and OFF aIF2 at resolution of 3.0 and 2.15 A
crystal structure analysis, overview
-
crystal structure of HflX from Sulfolobus solfataricus solved to 2.0 A resolution in apo- and GDP-bound forms
crystals of wild-type enzyme/GDP comple and mutant enzymes G235P and G235S are grown using hanging drop method at 16°C
elongation factor 1alpha in complex with GDP, structure at 1.8 A resolution
-
elongation factor 1alpha in complex with Mg2+ (100 mM) and GDP. Elongation factor 1alpha in complex with GDP does not bind Mg2+, when the ion is present in the crystallization medium at moderate concentrations (5 mM). Crystals are grown using PEG 4000 and propan-2-ol as precipitants. Diffraction quality crystals are obtained using microbatch under oil technique at 4°C and a protein concentration of 6 mg/ml
-
Fourier transform infrared spectroscopic study. Substitution of the GDP bound with guanyl-5'-yl imido diphosphate induces a slight increase in the alpha helix and beta sheet content. The alpha helix content of the enzyme-GDP complex increases upon addition of salts, and the highest effect is produced by 5 M NaCl. Thermal stability of the enzyme-GDP complex is significantly reduced when the GDP is replaced with guanyl-5'-yl imido diphosphate or in the presence of NaBr or NH4Cl
-
full-sized alphabetagamma heterotrimeric aIF2 in the nucleotide-free form, and aIF2alphagamma dimer, X-ray diffraction structure determination and analysis at 2.8 A resolution
wild-type and mutant enzyme subunit gamma in complex with GTP, GDP, or GDP analogues, with Mg2+, X-ray diffraction structure determination and analysis at 1.3-1.94 A resolution
crystal structure of the Mg2+-GDP complex of the Ffh NG-domain refined at 2.1 Å resolution
-
EF-Tu bound to aminoacyl-tRNA of the 70s ribosome and a GTP analogue, X-ray diffraction structure determination and analysis at 3.1 A resolution
-
purified recombinant apo-enzyme IF2 and its complex with GDP, vapor diffusion, mixing of 25 mg/ml protein in 30 mM HEPES-KOH, pH 7.5, 10 mM MgCl2, 30 mM NH4Cl, 1 mM EDTA NaOH, and 1 mM 2-mercaptoethanol in a 4:1 ratio with a well solution contaning 0.1 M calcium acetate, 0.04 M Na-cacodylate, pH 5.4, 8% w/v PEG 8000, 10-30 mM glycl-glycine, and 10-30 mM taurine, 2 weeks, X-ray diffraction structure determination and analysis aat 3.09 A resolution
purified recombinant apoenzyme protein core and enzyme in complex with GTP or GDP, sitting-drop vapour diffusion method, mixing of protein in 20 mM HEPES, pH 7.5, 50 mM KCl, 20 mM MgCl2, 1 mM DTT, with 2.5% glycerol and with reservoir solution containing 20% PEG 3350 and 0.2 M ammonium nitrate, to a final volume of 0.008 ml, 21°C, 1-3 weeks, X-ray diffraction structure determination and analysis
purified ribosomal protein L9-elongation factor G fusion protein in complex with GDP, the EF-G-GTP complex is bound on a pre-translocation ribosome (PRE ribosome) that is deficient in tRNA translocation upon EF-G binding, sitting drop vapour diffusion method, mixing of 0.1 mM protein in 10 mM Tris-HCl, pH 7.5, 200 mM KCl, 10 mM Mg(CH3COO)2, and 1 mM 2-mercaptoethanol, with X-ray diffraction structure determination and analysis at 2.0 A resolution. Only in the presence of the GDP nucleotide, and not GTP, does EF-G crystalize with the non-rotated ribosome under the experimental conditions
structure of the mutant enzyme T84A in complex with the non-hydrolysable GTP analogue GDPNP
-