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Information on EC 3.6.5.3 - protein-synthesizing GTPase and Organism(s) Saccharolobus solfataricus and UniProt Accession Q980A5

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IUBMB Comments
This enzyme comprises a family of proteins involved in prokaryotic as well as eukaryotic protein synthesis. In the initiation factor complex, it is IF-2b (98 kDa) that binds GTP and subsequently hydrolyses it in prokaryotes. In eukaryotes, it is eIF-2 (150 kDa) that binds GTP. In the elongation phase, the GTP-hydrolysing proteins are the EF-Tu polypeptide of the prokaryotic transfer factor (43 kDa), the eukaryotic elongation factor EF-1alpha (53 kDa), the prokaryotic EF-G (77 kDa), the eukaryotic EF-2 (70-110 kDa) and the signal recognition particle that play a role in endoplasmic reticulum protein synthesis (325 kDa). EF-Tu and EF-1alpha catalyse binding of aminoacyl-tRNA to the ribosomal A-site, while EF-G and EF-2 catalyse the translocation of peptidyl-tRNA from the A-site to the P-site. GTPase activity is also involved in polypeptide release from the ribosome with the aid of the pRFs and eRFs.
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Saccharolobus solfataricus
UNIPROT: Q980A5
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Word Map
The taxonomic range for the selected organisms is: Saccharolobus solfataricus
The enzyme appears in selected viruses and cellular organisms
Synonyms
elongation factor, translation initiation factor, gtpase-activating protein, eif2alpha, eif2b, elongation factor tu, eef1a, ef-1alpha, eukaryotic initiation factor 2, elongation factor g, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
archaeal initiation factor 2
-
archaeal translation initiation factor 2
-
initiation factor 2
-
translation initiation factor 2
-
archaeal initiation factor 2
-
-
EF-1alpha
elongation factor (EF)
-
-
-
-
elongation factor 1 alpha
-
-
elongation factor 1alpha
elongation factor 2
-
-
elongation factor-1alpha
-
elongation factor-1beta
-
elongation factor-2
-
GTP phosphohydrolase
-
-
-
-
GTPase
-
-
-
-
GTPase HflX
guanine triphosphatase
-
-
-
-
guanosine 5'-triphosphatase
-
-
-
-
guanosine triphosphatase
-
-
-
-
initiation factor (IF)
-
-
-
-
peptide-release or termination factor
-
-
-
-
protein-synthesizing GTPase
-
-
protein-sythesizing GTPase
ribosomal GTPase
-
-
-
-
ribosome-dependent GTPase
-
-
SsEF-1alpha
SSO0412
Q97W59; Q980A5; Q97Z79
locus name, gamma-subunit
SSO1050
Q97W59; Q980A5; Q97Z79
locus name, alpha-subunit
SSO2381
Q97W59; Q980A5; Q97Z79
locus name, beta-subunit
translation factor aIF2/5B
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
SYSTEMATIC NAME
IUBMB Comments
GTP phosphohydrolase (mRNA-translation-assisting)
This enzyme comprises a family of proteins involved in prokaryotic as well as eukaryotic protein synthesis. In the initiation factor complex, it is IF-2b (98 kDa) that binds GTP and subsequently hydrolyses it in prokaryotes. In eukaryotes, it is eIF-2 (150 kDa) that binds GTP. In the elongation phase, the GTP-hydrolysing proteins are the EF-Tu polypeptide of the prokaryotic transfer factor (43 kDa), the eukaryotic elongation factor EF-1alpha (53 kDa), the prokaryotic EF-G (77 kDa), the eukaryotic EF-2 (70-110 kDa) and the signal recognition particle that play a role in endoplasmic reticulum protein synthesis (325 kDa). EF-Tu and EF-1alpha catalyse binding of aminoacyl-tRNA to the ribosomal A-site, while EF-G and EF-2 catalyse the translocation of peptidyl-tRNA from the A-site to the P-site. GTPase activity is also involved in polypeptide release from the ribosome with the aid of the pRFs and eRFs.
CAS REGISTRY NUMBER
COMMENTARY hide
9059-32-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
GTP + H2O
GDP + phosphate
show the reaction diagram
GTP + H2O
GDP + phosphate
show the reaction diagram
guanylyl imidodiphosphate + H2O
?
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
GTP + H2O
GDP + phosphate
show the reaction diagram
GTP + H2O
GDP + phosphate
show the reaction diagram
guanylyl imidodiphosphate + H2O
?
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
zinc-binding domain in the beta-subunit
BaCl2
-
10 mM, about 8fold stimulation
CaCl2
-
10 mM, highest stimulation by BaCl2 (8fold), followed by SrCl2, MgCl2, MnCl2, CaCl2 and CoCl2 in a decreasing order of effectiveness
CoCl2
-
10 mM, highest stimulation by BaCl2 (8fold), followed by SrCl2, MgCl2, MnCl2, CaCl2 and CoCl2 in a decreasing order of effectiveness
MgCl2
-
10 mM, highest stimulation by BaCl2 (8fold), followed by SrCl2, MgCl2, MnCl2, CaCl2 and CoCl2 in a decreasing order of effectiveness
MnCl2
-
10 mM, highest stimulation by BaCl2 (8fold), followed by SrCl2, MgCl2, MnCl2, CaCl2 and CoCl2 in a decreasing order of effectiveness
NaCl
-
GTPase activity is measured in the presence of 3.6 M NaCl
SrCl2
-
10 mM, highest stimulation by BaCl2 (8fold), followed by SrCl2, MgCl2, MnCl2, CaCl2 and CoCl2 in a decreasing order of effectiveness
additional information
-
GTPase stimulated by ethylene glycol and BaCl2 does not require the presence of univalent cations. Li+, Na+, K+ or NH4+ added singularly up to 1 M concentration, do not produce any significant stimulation of SsEF-2 GTPase either in the absence or in the presence of ethylene glycol. They reduce the stimulation of SsEF-2 GTPase by ethylene glycol plus BaCl2 or SrCl2
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
GE2270A
guanidine hydrochloride
-
deactivation by denaturation of the protein
guanosine 5'-(beta,gamma-imido)triphosphate
-
-
guanosine 5'-tetraphosphate
-
competitive inhibition of intrinsic GTPase, inhibition of archaeal protein synthesis in vitro, even though the concentration required to get inhibition is higher than that required for the eubacterial and eukaryal systems
guanosine-5'-[(beta,gamma)-imido]triphosphate
-
i.e. GppNHp. GTPase activity in the presence of a molar concentration of NaCl is competitively inhibited
guanyl-5'-yl imidodiphosphate
-
competitive with GTP
guanyl-5'-yl imidotriphosphate
-
-
pulvomycin
-
the antibiotic is able to reduce in vitro the rate of protein synthesis however, the concentration of pulvomycin leading to 50% inhibition (173 mM) is two order of magnitude higher but one order lower than that required in eubacteria and eukarya, respectively. Pulvomycin is able to decrease the affinity of the elongation factor toward aa-tRNA only in the presence of GTP, to an extent similar to that measured in the presence of GDP
tetracycline
-
mixed inhibition. The inhibition level depends on the antibiotic concentration, even though a complete inhibition is not reached even in the presence of 0.120 mM antibiotic, a concentration corresponding to about 200fold molar excess over the elongation factor
Urea
-
deactivation by denaturation of the protein
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-propanol
-
stimulation by aliphatic alcohols in a decreasing order of effectiveness: ethylene glycol > 2-propanol > ethanol > glycerol > methanol > 1-propanol
2-propanol
-
stimulation by aliphatic alcohols in a decreasing order of effectiveness: ethylene glycol > 2-propanol > ethanol > glycerol > methanol > 1-propanol
ethanol
-
stimulation by aliphatic alcohols in a decreasing order of effectiveness: ethylene glycol > 2-propanol > ethanol > glycerol > methanol > 1-propanol
ethylene glycoI
-
60%, 300fold stimulation
glycerol
-
stimulation by aliphatic alcohols in a decreasing order of effectiveness: ethylene glycol > 2-propanol > ethanol > glycerol > methanol > 1-propanol
kirromycin
-
enhances activity of mutant enzyme G13A (maximal stimulation at 0.04 mM), does not stimulate intrinsic GTPase of SsEF-1alpha triggered by 3.6 M NaCl
methanol
-
stimulation by aliphatic alcohols in a decreasing order of effectiveness: ethylene glycol > 2-propanol > ethanol > glycerol > methanol > 1-propanol
pulvomycin
-
increasing pulvomycin concentration increased the rate of the intrinsic GTPase catalysed by elongation factor 1alpha, reaching its maximum stimulation effect at 30 mM. Pulvomycin exerts its stimulatory function at all the tested temperatures (45-75°C).
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0008 - 0.148
GTP
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0004 - 8.8
GTP
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.048 - 177
GTP
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00012 - 0.0074
GDP
0.0084 - 0.0407
guanosine 5'-(beta,gamma-imido)triphosphate
0.00047
guanosine-5'-[(beta,gamma)-imido]triphosphate
-
pH 7.8, 50°C, GTPase activity in the presence 3.6 M NaCl
0.0084 - 0.0407
guanyl-5'-yl imidotriphosphate
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0059 - 0.0463
GE2270A
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
90
-
wild-type enzyme
additional information
-
the rate of nucleotide binding to aEF-1 a increased with temperature, reaching a maximum at 95°C
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70 - 86
-
about 60% of maximal activity at 70°C and at 86°C, mutant enzyme G13A
70 - 95
-
70°C: about 60% of maximal activity, 95°C: about 90% of maximal activity, wild-type enzyme
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
physiological function
-
the universally conserved GTPase HflX is a putative translation factor whose GTPase activity is stimulated by the 70S ribosome as well as the 50S but not the 30S ribosomal subunit
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28000
-
truncated G-form of SsEF-1alpha, determined by SDS-PAGE and Western blot
38000
-
truncated GM-form of SsEF-1alpha, determined by SDS-PAGE and Western blot
49000
50500
-
x * 50500, His6-tagged Hflx, SDS-PAGE
70000
-
x * 70000, His-tagged protein, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterotrimer
aIF2 is composed of three subunits, alpha, bbeta, and gamma. The gamma subunit forms the core of the heterotrimer and contains the GTP-binding pocket. alpha and beta are bound to subunit gamma but do not interact together. The gamma subunit closely resembles elongation factor EF1A
trimer
heterotrimer, the archaeal factor aIF2 is formed upon the 1:1:1 association of three subunits: alpha, beta, and gamma
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
differently from the wild-type enzyme the recombinant enzyme does not undergo post-translational modification of His603 into diphthamide, as indicated by its inability to be ADP-ribosylated
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
analysis of crystal structures of ON and OFF aIF2 at resolution of 3.0 and 2.15 A
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
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
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D19A
site-directed mutagenesis, the mutation does not strongly modify the GDP binding properties of the two mutant enzyme, but reduces the GTP hydrolysis rate
D19A/H97A
site-directed mutagenesis, almost inactive mutant
H97A
site-directed mutagenesis, the mutation does not strongly modify the GDP binding properties of the two mutant enzyme, but reduces the GTP hydrolysis rate
D60A
-
1.4fold slower hydrolysis of GTP
F236P
kcat/Km is 63% compared to wild-type value
G13A
-
compared to wild-type enzyme the mutant shows a reduced rate of Phe polymerization and a reduced intrinsic GTPase activity that is stimulated by high concentrations of NaCl. Mutant enzyme shows an increased affinity for GTP and GDP. The temperature inducing a 50% denaturation of the mutant enzyme is 5°C lower than that of the wild-type enzyme
G235P
complete loss of GTP hydrolyzing activity
G235S
partial loss of GTP hydrolyzing activity
N189P
complete loss of GTP hydrolyzing activity
Ss(G)EF-1alpha
-
truncated form of SsEF-1alpha
Ss(GM)EF-1alpha
-
truncated form of SsEF-1alpha
T193N
complete loss of GTP hydrolyzing activity
T213V
kcat is 45% compared to the wild-type value
Y54H
the mutant of isoform EF-1beta shows wild type activity
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
105
the enzyme isoform EF-1beta retains 50% activity after 30 min at 105°C
20 - 100
-
EF-1alpha denaturation profile at pH 4.0, the protonation state of the numerous Asp and Glu residues plays a critical role for the thermally denatured state of the enzyme, reversibility of the inter-conversion between the two denatured forms, overview
87 - 96
-
half-inactivation time 99 min at 87°C, half-inactivation time 3.5 min at 96°C
91
-
10 min, 50% inactivation of GDP binding ability, mutant enzyme G13A
92
-
half-denaturation of wild-type enzyme
93.6
-
temperature for half denaturation of D60A mutant
94
-
10 min, 50% inactivation of GDP binding ability, wild-type enzyme
95
-
10 min, 50% inactivation
95.1
-
temperature for half denaturation
96
-
binding of guanosine 5'-tetraphosphate to SsEF-1alpha renders the elongation factor more resistant to heat treatment. The denaturation profile of the elongation factor in the presence of guanosine tetraphosphate is shifted towards higher temperatures with a denaturation midpoint (96.4°C) about 2°C higher with respect to that observed for the elongation factor bound to GDP
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
conformational change of the elongation factor takes place upon interaction with the antibiotic. Protection against chemical denaturation of SsEF-1alpha is observed in the presence of pulvomycin
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
guanidine-HCl
-
50% inactivation of GTPase activity at 3.0 M guanidine-HCl in presence 3.6 M NaCl and absence of pulvomycin. 50% inactivation of GTPase activity at 3.6 M guanidine-HCl in presence 3.6 M NaCl and presence of pulvomycin
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 20 mM Tris/HCl, pH 7.8, 50 mM KCl, 10 mM MgCl2, 50% v/v glycerol
-
-20°C, stable for several months
-
-20°C, Tris/HCl buffer, pH 7.8, 10 mM MgCl2, 50 mM KCl, 50% v/v glycerol
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
comparison of sequence with that of Sulfolobus solfataricus strain MT4 shows only one amino acid change, i.e. I15V. The difference is in the first guanine nucleotide binding consensus sequence G13HIDHGK and is responsible for a increased efficiency in protein synthesis, which is accompanied by an reduced affinity for both guanosine diphosphate (GDP) and guanosine triphosphate (GTP), and an decreased efficiency in the intrinsic GTPase activity
comparison of sequence with that of Sulfolobus solfataricus strain MT4 shows only one amino acid change, i.e. V15I. The difference is in the first guanine nucleotide binding consensus sequence G13HIDHGK and is responsible for a reduced efficiency in protein synthesis, which is accompanied by an increased affinity for both guanosine diphosphate (GDP) and guanosine triphosphate (GTP), and an increased efficiency in the intrinsic GTPase activity
expressed in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli BL21
-
expression in Escherichia coli using the pT7-7 expression vector
-
for expression in Escherichia coli cells
-
recombinant SsEF-1alpha and its nucleotide-free form are prepared by using an Escherichia coli expression system
-
the gene encoding SsEF-1alpha from the strain MT3 is cloned, sequenced and expressed in Escherichia coli, the vectors pGEM-3Z and pET22 are used
the SsEF-1alpha gene is cloned into the pT7-7 vector for expression in Escherichia coli BL21DE3 cells, in addition two truncated forms of SsEF-1alpha are constructed, encoding the domain G and the domains G+M
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
denaturation by urea and guanidine hydrochloride shows a cooperative unfolding process with no intermediate species. Chemical unfolding by urea and guanidine hydrochloride is fully reversible for both enzyme-GDP complex and nucleotide-free enzyme. Both forms exhibit remarkable stability against urea, but not against guanidine hydrochloride
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Raimo, G.; Masullo, M.; Lombardo, B.; Bocchini, V.
The archaeal elongation factor 1alpha bound to GTP forms a ternary complex with eubacterial and aukaryal aminoacyl-tRNA
Eur. J. Biochem.
267
6012-6017
2000
Saccharolobus solfataricus
Manually annotated by BRENDA team
Masullp, M.; De Vendittis, E.; Bocchini, V.
Archaebacterial elongation factor 1 alpha carries the catalytic site for GTP hydrolysis
J. Biol. Chem.
269
20376-20379
1994
Saccharolobus solfataricus
Manually annotated by BRENDA team
Masullo, M.; Cantiello, P.; de Paola, B.; Catanzano, F.; Arcari, P.; Bocchini, V.
G13A substitution affects the biochemical and physical properties of the elongation factor 1 alpha. A reduced intrinsic GTPase activity is partially restored by kirromycin
Biochemistry
41
628-633
2002
Saccharolobus solfataricus
Manually annotated by BRENDA team
Vitagliano, L.; Masullo, M.; Sica, F.; Zagari, A.; Bocchini, V.
The crystal structure of Sulfolobus solfataricus elongation factor 1alpha in complex with GDP reveals novel features in nucleotide binding and exchange
EMBO J.
20
5305-5311
2001
Saccharolobus solfataricus
Manually annotated by BRENDA team
Vitagliano, L.; Ruggiero, A.; Masullo, M.; Cantiello, P.; Arcari, P.; Zagari, A.
The crystal structure of Sulfolobus solfataricus elongation factor 1alpha in complex with magnesium and GDP
Biochemistry
43
6630-6636
2004
Saccharolobus solfataricus
Manually annotated by BRENDA team
Tanfani, F.; Scire, A.; Masullo, M.; Raimo, G.; Bertoli, E.; Bocchini, V.
Salts induce structural changes in elongation factor 1alpha from the hyperthermophilic archaeon Sulfolobus solfataricus: a Fourier transform infrared spectroscopic study
Biochemistry
40
13143-13148
2001
Saccharolobus solfataricus
Manually annotated by BRENDA team
Granata, V.; Graziano, G.; Ruggiero, A.; Raimo, G.; Masullo, M.; Arcari, P.; Vitagliano, L.; Zagari, A.
Chemical denaturation of the elongation factor 1alpha isolated from the hyperthermophilic archaeon Sulfolobus solfataricus
Biochemistry
45
719-726
2006
Saccharolobus solfataricus
Manually annotated by BRENDA team
Masullo, M.; Ianniciello, G.; Arcari, P.; Bocchini, V.
Properties of truncated forms of the elongation factor 1alpha from the archaeon Sulfolobus solfataricus
Eur. J. Biochem.
243
468-473
1997
Saccharolobus solfataricus
Manually annotated by BRENDA team
De Vendittis, E.; Adinolfi, B.S.; Amatruda, M.R.; Raimo, G.; Masullo, M.; Bocchini, V.
The A26G replacement in the consensus sequence A-X-X-X-X-G-K-[T,S] of the guanine nucleotide binding site activates the intrinsic GTPase of the elongation factor 2 from the archaeon Sulfolobus solfataricus
Eur. J. Biochem.
262
600-605
1999
Saccharolobus solfataricus
Manually annotated by BRENDA team
Masullo, M.; Cantiello, P.; Arcari, P.
Archaeal elongation factor 1alpha from Sulfolobus solfataricus interacts with the eubacterial antibiotic GE2270A
Extremophiles
8
499-505
2004
Saccharolobus solfataricus
Manually annotated by BRENDA team
Masullo, M.; Cantiello, P.; Lamberti, A.; Longo, O.; Fiengo, A.; Arcari, P.
Cloning, expression and evolution of the gene encoding the elongation factor 1alpha from a low thermophilic Sulfolobus solfataricus strain
FEMS Microbiol. Lett.
218
285-290
2003
Saccharolobus solfataricus, Saccharolobus solfataricus (P35021)
Manually annotated by BRENDA team
Raimo, G.; Masullo, M.; Bocchini, V.
Studies on the polypeptide elongation factor 2 from Sulfolobus solfataricus. Interaction with guanosine nucleotides and GTPase activity stimulated by ribosomes
J. Biol. Chem.
270
21082-21085
1995
Saccharolobus solfataricus
Manually annotated by BRENDA team
Granata, V.; Graziano, G.; Ruggiero, A.; Raimo, G.; Masullo, M.; Arcari, P.; Vitagliano, L.; Zagari, A..
Stability against temperature of Sulfolobus solfataricus elongation factor 1alpha, a multi-domain protein
Biochim. Biophys. Acta
1784
573-581
2008
Saccharolobus solfataricus
Manually annotated by BRENDA team
Stolboushkina, E.; Nikonov, S.; Nikulin, A.; Blaesi, U.; Manstein, D.J.; Fedorov, R.; Garber, M.; Nikonov, O.
Crystal structure of the intact archaeal translation initiation factor 2 demonstrates very high conformational flexibility in the alpha- and beta-subunits
J. Mol. Biol.
382
680-691
2008
Saccharolobus solfataricus (Q980A5), Saccharolobus solfataricus
Manually annotated by BRENDA team
Ruggiero, I.; Cantiello, P.; Lamberti, A.; Sorrentino, A.; Martucci, N.M.; Ruggiero, A.; Arcone, R.; Vitagliano, L.; Arcari, P.; Masullo, M.
Biochemical characterisation of the D60A mutant of the elongation factor 1alpha from the archaeon Sulfolobus solfataricus
Biochimie
91
835-842
2009
Saccharolobus solfataricus
Manually annotated by BRENDA team
Satpati, P.; Simonson, T.
Conformational selection by the aIF2 GTPase: a molecular dynamics study of functional pathways
Biochemistry
51
353-361
2012
Saccharolobus solfataricus
Manually annotated by BRENDA team
Fischer, J.J.; Coatham, M.L.; Eagle Bear, S.; Brandon, H.E.; De Laurentiis, E.I.; Shields, M.J.; Wieden, H.J.
The ribosome modulates the structural dynamics of the conserved GTPase HflX and triggers tight nucleotide binding
Biochimie
94
1647-1659
2012
Saccharolobus solfataricus
Manually annotated by BRENDA team
Satpati, P.; Clavaguera, C.; Ohanessian, G.; Simonson, T.
Free energy simulations of a GTPase: GTP and GDP binding to archaeal initiation factor 2
J. Phys. Chem. B
115
6749-6763
2011
Saccharolobus solfataricus (Q980A5)
Manually annotated by BRENDA team
Raimo, G.; Masullo, M.; Scarano, G.; Bocchini, V.
The site for GTP hydrolysis on the archaeal elongation factor 2 is unmasked by aliphatic alcohols
Biochimie
78
832-837
1996
Saccharolobus solfataricus, Saccharolobus solfataricus ATCC 49255
Manually annotated by BRENDA team
de Vendittis, E.; Amatruda, M.R.; Raimo, G.; Bocchini, V.
Heterologous expression in Escherichia coli of the gene encoding an archaeal thermoacidophilic elongation factor 2. Properties of the recombinant protein
Biochimie
79
303-308
1997
Saccharolobus solfataricus
Manually annotated by BRENDA team
Martucci, N.M.; Lamberti, A.; Arcari, P.; Masullo, M.
The eubacterial protein synthesis inhibitor pulvomycin interacts with archaeal elongation factor 1alpha from Sulfolobus solfataricus
Biochimie
94
503-509
2012
Saccharolobus solfataricus
Manually annotated by BRENDA team
Lamberti, A.; Martucci, N.M.; Ruggiero, I.; Arcari, P.; Masullo, M.
Interaction between the antibiotic tetracycline and the elongation factor 1alpha from the archaeon Sulfolobus solfataricus
Chem. Biol. Drug Des.
78
260-268
2011
Saccharolobus solfataricus
Manually annotated by BRENDA team
Masullo, M.; Raimo, G.; Parente, A.; Gambacorta, A.; De Rosa, M.; Bocchini, V.
Properties of the elongation factor 1 alpha in the thermoacidophilic archaebacterium Sulfolobus solfataricus
Eur. J. Biochem.
199
529-537
1991
Saccharolobus solfataricus, Saccharolobus solfataricus MT-4 / DSM 5833
Manually annotated by BRENDA team
Martucci, N.M.; Lamberti, A.; Vitagliano, L.; Cantiello, P.; Ruggiero, I.; Arcari, P.; Masullo, M.
The magic spot ppGpp influences in vitro the molecular and functional properties of the elongation factor 1alpha from the archaeon Sulfolobus solfataricus
Extremophiles
16
743-749
2012
Saccharolobus solfataricus
Manually annotated by BRENDA team
Blombach, F.; Launay, H.; Zorraquino, V.; Swarts, D.C.; Cabrita, L.D.; Benelli, D.; Christodoulou, J.; Londei, P.; van der Oost, J.
An HflX-type GTPase from Sulfolobus solfataricus binds to the 50S ribosomal subunit in all nucleotide-bound states
J. Bacteriol.
193
2861-2867
2011
Saccharolobus solfataricus (Q980M3), Saccharolobus solfataricus P2 (Q980M3)
Manually annotated by BRENDA team
Huang, B.; Wu, H.; Hao, N.; Blombach, F.; van der Oost, J.; Li, X.; Zhang, X.C.; Rao, Z.
Functional study on GTP hydrolysis by the GTP-binding protein from Sulfolobus solfataricus, a member of the HflX family
J. Biochem.
148
103-113
2010
Saccharolobus solfataricus (Q980M3), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q980M3)
Manually annotated by BRENDA team
Maone, E.; Di Stefano, M.; Berardi, A.; Benelli, D.; Marzi, S.; La Teana, A.; Londei, P.
Functional analysis of the translation factor aIF2/5B in the thermophilic archaeon Sulfolobus solfataricus
Mol. Microbiol.
65
700-713
2007
Saccharolobus solfataricus
Manually annotated by BRENDA team
Schmitt, E.; Panvert, M.; Lazennec-Schurdevin, C.; Coureux, P.D.; Perez, J.; Thompson, A.; Mechulam, Y.
Structure of the ternary initiation complex aIF2-GDPNP-methionylated initiator tRNA
Nat. Struct. Mol. Biol.
19
450-454
2012
Saccharolobus solfataricus (Q97W59 and Q980A5 and Q97Z79), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q97W59 and Q980A5 and Q97Z79)
Manually annotated by BRENDA team
Wu, H.; Sun, L.; Blombach, F.; Brouns, S.J.; Snijders, A.P.; Lorenzen, K.; van den Heuvel, R.H.; Heck, A.J.; Fu, S.; Li, X.; Zhang, X.C.; Rao, Z.; van der Oost, J.
Structure of the ribosome associating GTPase HflX.
Proteins
78
705-713
2010
Saccharolobus solfataricus (Q980M3), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q980M3)
Manually annotated by BRENDA team
Bocchini, V.; Adinolfi, B.S.; Arcari, P.; Arcucci, A.; Dello Russo, A.; De Vendittis, E.; Ianniciello, G.; Masullo, M.; Raimo, G.
Protein engineering on enzymes of the peptide elongation cycle in Sulfolobus solfataricus
Biochimie
80
895-898
1998
Saccharolobus solfataricus (P30925), Saccharolobus solfataricus (P35021), Saccharolobus solfataricus (Q64214)
Manually annotated by BRENDA team
Dubiez, E.; Aleksandrov, A.; Lazennec-Schurdevin, C.; Mechulam, Y.; Schmitt, E.
Identification of a second GTP-bound magnesium ion in archaeal initiation factor 2
Nucleic Acids Res.
43
2946-2957
2015
Saccharolobus solfataricus (Q980A5), Saccharolobus solfataricus P2 (Q980A5), Saccharolobus solfataricus JCM 11322 (Q980A5), Saccharolobus solfataricus ATCC 35092 (Q980A5), Saccharolobus solfataricus DSM 1617 (Q980A5)
Manually annotated by BRENDA team