Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.6.5.3 - protein-synthesizing GTPase

for references in articles please use BRENDA:EC3.6.5.3
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
UNIPROT: P0CE47
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The enzyme appears in 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
elongation factor (EF)
-
-
-
-
GTP phosphohydrolase
-
-
-
-
GTPase
-
-
-
-
guanine triphosphatase
-
-
-
-
guanosine 5'-triphosphatase
-
-
-
-
guanosine triphosphatase
-
-
-
-
initiation factor (IF)
-
-
-
-
peptide-release or termination factor
-
-
-
-
ribosomal GTPase
-
-
-
-
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
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
-
-
-
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
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
kirromycin
KIR, an antibiotic that directly binds to the interface of EF-Tu domains D1 and D3 and prevents dissociation of EF-Tu from the ribosome and from the amino acid-tRNA after GTP hydrolysis. Kirromycin binds within the D1-D3 interface, sterically blocking its closure, but does not prevent hydrolysis. With KIR bound, the overall conformation of EF-Tu remains close to the GTP-bound conformation after hydrolysis, both on and off the ribosome
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
elongation factor Tu (EF-Tu) is a central part of the bacterial translation machinery. During each round of translation elongation, EF-Tu delivers an aminoacyl-tRNA (aatRNA) to the ribosome in a ternary complex with GTP. The successful decoding of the messenger RNA codon by the aa-tRNA leads to a closing of the small ribosomal subunit (30S), which in turn docks EF-Tu at the sarcin-ricin loop of the large subunit (50S) in the GTPase-activated (GA) state. The transition of EF-Tu into a reorganized catalytic configuration in the GTPase-activated state catalyzes GTP hydrolysis to GDP, followed by the release of inorganic phosphate (Pi) and a conformational change of EF-Tu
additional information
EF-Tu in the GTPase-activated conformation, three-dimensional structure. The gamma-phosphate of GTP interacts with EF-Tu via the P-loop (V20, D21), the switch 1 loop (T61), and the switch 2 loop (G83). The switch 1 loop in turn is involved in the binding of EF-Tu to the tRNA (nucleotides 1-3 and 73-75). The conformational changes of the ribosome-EF-Tu complex and the effect of GTP hydrolysis as well as of KIR are modeled by all-atom explicit-solvent molecular dynamics simulations with GTP and with GDP and KIR as well as with GDP in the absence of KIR
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
EFTU1_ECOLI
Escherichia coli (strain K12)
394
0
43284
Swiss-Prot
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Warias, M.; Grubmueller, H.; Bock, L.V.
tRNA dissociation from EF-Tu after GTP hydrolysis primary steps and antibiotic inhibition
Biophys. J.
117
1-11
2019
Escherichia coli (P0CE47), Thermus aquaticus (Q01698)
Manually annotated by BRENDA team